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Clathrin

April 08, 2024

Clathrin is a protein that plays a major role in the formation of coated vesicles. Clathrin was first isolated by Barbara Pearse in 1976.[1] It forms a triskelion shape composed of three clathrin heavy chains and three light chains. When the triskelia interact they form a polyhedral lattice that surrounds the vesicle. The protein's name refers to this lattice structure, deriving from Latin clathri meaning lattice.[2] Barbara Pearse named the protein clathrin at the suggestion of Graeme Mitchison, selecting it from three possible options.[3] Coat-proteins, like clathrin, are used to build small vesicles in order to transport molecules within cells. The endocytosis and exocytosis of vesicles allows cells to communicate, to transfer nutrients, to import signaling receptors, to mediate an immune response after sampling the extracellular world, and to clean up the cell debris left by tissue inflammation. The endocytic pathway can be hijacked by viruses and other pathogens in order to gain entry to the cell during infection.[4]

Clathrin heavy N-terminal propeller repeat
Clathrin terminal domain
Identifiers
SymbolClathrin_propel
PfamPF01394
Pfam clanCL0020
InterProIPR022365
SCOP21bpo / SCOPe / SUPFAM
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary
Clathrin heavy-chain linker
clathrin heavy chain proximal repeat (linker)
Identifiers
SymbolClathrin-link
PfamPF09268
Pfam clanCL0020
InterProIPR015348
SCOP21b89 / SCOPe / SUPFAM
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary
CHCR/VPS 7-fold repeat
Identifiers
SymbolClathrin_propel
PfamPF00637
Pfam clanCL0020
InterProIPR000547
SMARTSM00299
PROSITEPS50236
CATH1b89
SCOP21b89 / SCOPe / SUPFAM
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary
Clathrin light chain
Identifiers
SymbolClathrin_lg_ch
PfamPF01086
InterProIPR000996
PROSITEPDOC00196
SCOP23iyv / SCOPe / SUPFAM
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary

Structure edit

Clathrin light chain a
Identifiers
SymbolCLTA
NCBI gene1211
HGNCCLTA. HGNC:2090. CLTA.
UniProtP09496
Other data
LocusChr. 9 q13
Search for
StructuresSwiss-model
DomainsInterPro
Clathrin light chain b
Identifiers
SymbolCLTB
NCBI gene1212
HGNC2091
OMIM118970
RefSeqNM_001834
UniProtP09497
Other data
LocusChr. 5 q35
Search for
StructuresSwiss-model
DomainsInterPro
Clathrin heavy chain 1
Identifiers
SymbolCLTC
Alt. symbolsCHC, CHC17, CLTCL2
NCBI gene1213
HGNC2092
OMIM118955
RefSeqNM_004859
UniProtQ00610
Other data
LocusChr. 17 q23.1-qter
Search for
StructuresSwiss-model
DomainsInterPro
Clathrin heavy chain 2
Identifiers
SymbolCLTCL1
Alt. symbolsCLTCL
NCBI gene8218
HGNC2093
OMIM601273
RefSeqNM_001835
UniProtP53675
Other data
LocusChr. 22 q11.21
Search for
StructuresSwiss-model
DomainsInterPro

The clathrin triskelion is composed of three clathrin heavy chains interacting at their C-termini, each ~190 kDa heavy chain has a ~25 kDa light chain tightly bound to it. The three heavy chains provide the structural backbone of the clathrin lattice, and the three light chains are thought to regulate the formation and disassembly of a clathrin lattice. There are two forms of clathrin light chains, designated a and b. The main clathrin heavy chain, located on chromosome 17 in humans, is found in all cells. A second clathrin heavy chain gene, on chromosome 22, is expressed in muscle.[5]

Clathrin heavy chain is often described as a leg, with subdomains, representing the foot (the N-terminal domain), followed by the ankle, distal leg, knee, proximal leg, and trimerization domains. The N-terminal domain consists of a seven-bladed β-propeller structure. The other domains form a super-helix of short alpha helices. This was originally determined from the structure of the proximal leg domain that identified and is composed of a smaller structural module referred to as clathrin heavy chain repeat motifs. The light chains bind primarily to the proximal leg portion of the heavy chain with some interaction near the trimerization domain. The β-propeller at the 'foot' of clathrin contains multiple binding sites for interaction with other proteins.[5]

 
A clathrin cage with a single triskelion highlighted in blue. CryoEM map EMD_5119 was rendered in UCSF Chimera and one clathrin triskelion was highlighted.
 
Each cage has 12 pentagons. Mini-coat (left) has 4 hexagons and tetrahedral symmetry as in a truncated triakis tetrahedron. Hexagonal barrel (middle) has 8 hexagons and D6 symmetry. Soccer ball (right) has 20 hexagons and icosahedral symmetry as in a truncated icosahedron.

When triskelia assemble together in solution, they can interact with enough flexibility to form 6-sided rings (hexagons) that yield a flat lattice, or 5-sided rings (pentagons) that are necessary for curved lattice formation. When many triskelions connect, they can form a basket-like structure. The structure shown, is built of 36 triskelia, one of which is shown in blue. Another common assembly is a truncated icosahedron. To enclose a vesicle, exactly 12 pentagons must be present in the lattice.

In a cell, clathrin triskelion in the cytoplasm binds to an adaptor protein that has bound membrane, linking one of its three feet to the membrane at a time. Clathrin cannot bind to membrane or cargo directly and instead uses adaptor proteins to do this. This triskelion will bind to other membrane-attached triskelia to form a rounded lattice of hexagons and pentagons, reminiscent of the panels on a soccer ball, that pulls the membrane into a bud. By constructing different combinations of 5-sided and 6-sided rings, vesicles of different sizes may assemble. The smallest clathrin cage commonly imaged, called a mini-coat, has 12 pentagons and only two hexagons. Even smaller cages with zero hexagons probably do not form from the native protein, because the feet of the triskelia are too bulky.[6]

Function edit

 
Mechanism of clathrin-mediated endocytosis.

Clathrin performs critical roles in shaping rounded vesicles in the cytoplasm for intracellular trafficking. Clathrin-coated vesicles (CCVs) selectively sort cargo at the cell membrane, trans-Golgi network, and endosomal compartments for multiple membrane traffic pathways. After a vesicle buds into the cytoplasm, the coat rapidly disassembles, allowing the clathrin to recycle while the vesicle gets transported to a variety of locations.

Adaptor molecules are responsible for self-assembly and recruitment. Two examples of adaptor proteins are AP180[7] and epsin.[8][9][10] AP180 is used in synaptic vesicle formation. It recruits clathrin to membranes and also promotes its polymerization. Epsin also recruits clathrin to membranes and promotes its polymerization, and can help deform the membrane, and thus clathrin-coated vesicles can bud. In a cell, a triskelion floating in the cytoplasm binds to an adaptor protein, linking one of its feet to the membrane at a time. The triskelion foot will bind to other ones attached to the membrane to form a polyhedral lattice, triskelion foot, which pulls the membrane into a bud. The foot does not bind directly to the membrane, but binds to the adaptor proteins that recognize the molecules on the membrane surface.

Clathrin has another function aside from the coating of organelles. In non-dividing cells, the formation of clathrin-coated vesicles occurs continuously. Formation of clathrin-coated vesicles is shut down in cells undergoing mitosis. During mitosis, clathrin binds to the spindle apparatus, in complex with two other proteins: TACC3 and ch-TOG/CKAP5. Clathrin aids in the congression of chromosomes by stabilizing kinetochore fibers of the mitotic spindle. The amino-terminal domain of the clathrin heavy chain and the TACC domain of TACC3 make the microtubule binding surface for TACC3/ch-TOG/clathrin to bind to the mitotic spindle. The stabilization of kinetochore fibers requires the trimeric structure of clathrin in order to crosslink microtubules.[11][12][13]

Clathrin-mediated endocytosis (CME) regulates many cellular physiological processes such as the internalization of growth factors and receptors, entry of pathogens, and synaptic transmission. It is believed that cellular invaders use the nutrient pathway to gain access to a cell's replicating mechanisms. Certain signalling molecules open the nutrients pathway.[1] Two chemical compounds called Pitstop 1 and Pitstop 2, selective clathrin inhibitors, can interfere with the pathogenic activity, and thus protect the cells against invasion. These two compounds selectively block the endocytic ligand association with the clathrin terminal domain in vitro.[14] However, the specificity of these compounds to block clathrin-mediated endocytosis has been questioned.[15] In later studies, however, the specificity of Pitstop 2 was validated as being clathrin dependent.[16]

See also edit

References edit

  1. ^ a b Pearse BM (April 1976). "Clathrin: a unique protein associated with intracellular transfer of membrane by coated vesicles". Proceedings of the National Academy of Sciences of the United States of America. 73 (4): 1255–1259. Bibcode:1976PNAS...73.1255P. doi:10.1073/pnas.73.4.1255. PMC 430241. PMID 1063406.
  2. ^ "clathrate, adjective". Merriam-Webster. Retrieved 29 November 2023.
  3. ^ Pearse BM (September 1987). "Clathrin and coated vesicles". EMBO J. 6 (9): 2507–12. doi:10.1002/j.1460-2075.1987.tb02536.x. PMC 553666. PMID 2890519.
  4. ^ "InterPro". from the original on 2016-01-16. Retrieved 2015-10-07.
  5. ^ a b Robinson MS (December 2015). "Forty Years of Clathrin-coated Vesicles". Traffic. 16 (12): 1210–38. doi:10.1111/tra.12335. PMID 26403691.
  6. ^ Fotin A, Kirchhausen T, Grigorieff N, Harrison SC, Walz T, Cheng Y (December 2006). "Structure determination of clathrin coats to subnanometer resolution by single particle cryo-electron microscopy". J Struct Biol. 156 (3): 453–60. doi:10.1016/j.jsb.2006.07.001. PMC 2910098. PMID 16908193.
  7. ^ McMahon HT. . MRC Laboratory of Molecular Biology. Archived from the original on 2009-05-01. Retrieved 2009-04-17. micrographs of clathrin assembly
  8. ^ Ford MG, Pearse BM, Higgins MK, Vallis Y, Owen DJ, Gibson A, et al. (February 2001). (PDF). Science. 291 (5506): 1051–1055. Bibcode:2001Sci...291.1051F. CiteSeerX 10.1.1.407.6006. doi:10.1126/science.291.5506.1051. PMID 11161218. Archived from the original (PDF) on 2008-11-21. Retrieved 2009-04-17.
  9. ^ Higgins MK, McMahon HT (May 2002). (PDF). Trends in Biochemical Sciences. 27 (5): 257–263. doi:10.1016/S0968-0004(02)02089-3. PMID 12076538. Archived from the original (PDF) on 2008-11-21. Retrieved 2009-04-17.
  10. ^ Royle SJ, Bright NA, Lagnado L (April 2005). "Clathrin is required for the function of the mitotic spindle". Nature. 434 (7037): 1152–1157. Bibcode:2005Natur.434.1152R. doi:10.1038/nature03502. PMC 3492753. PMID 15858577.
  11. ^ Hood FE, Williams SJ, Burgess SG, Richards MW, Roth D, Straube A, et al. (August 2013). "Coordination of adjacent domains mediates TACC3-ch-TOG-clathrin assembly and mitotic spindle binding". The Journal of Cell Biology. 202 (3): 463–478. doi:10.1083/jcb.201211127. PMC 3734082. PMID 23918938.
  12. ^ Prichard KL, O'Brien NS, Murcia SR, Baker JR, McCluskey A (2022-01-18). "Role of Clathrin and Dynamin in Clathrin Mediated Endocytosis/Synaptic Vesicle Recycling and Implications in Neurological Diseases". Frontiers in Cellular Neuroscience. 15: 754110. doi:10.3389/fncel.2021.754110. PMC 8805674. PMID 35115907.
  13. ^ Role of the Clathrin Terminal Domain in Regulating Coated Pit Dynamics Revealed by Small Molecule Inhibition|Cell, Volume 146, Issue 3, 471-484, 5 August 2011 Abstract 2012-01-19 at the Wayback Machine
  14. ^ Dutta D, Williamson CD, Cole NB, Donaldson JG (Sep 2012). "Pitstop 2 is a potent inhibitor of clathrin-independent endocytosis". PLOS ONE. 7 (9): e45799. Bibcode:2012PLoSO...745799D. doi:10.1371/journal.pone.0045799. PMC 3448704. PMID 23029248.
  15. ^ Robertson MJ, Horatscheck A, Sauer S, von Kleist L, Baker JR, Stahlschmidt W, et al. (November 2016). "5-Aryl-2-(naphtha-1-yl)sulfonamido-thiazol-4(5H)-ones as clathrin inhibitors". Organic & Biomolecular Chemistry. 14 (47): 11266–11278. doi:10.1039/C6OB02308H. PMID 27853797.

Further reading edit

  • Wakeham DE, Chen CY, Greene B, Hwang PK, Brodsky FM (October 2003). "Clathrin self-assembly involves coordinated weak interactions favorable for cellular regulation". The EMBO Journal. 22 (19): 4980–4990. doi:10.1093/emboj/cdg511. PMC 204494. PMID 14517237.
  • Ford MG, Mills IG, Peter BJ, Vallis Y, Praefcke GJ, Evans PR, et al. (September 2002). "Curvature of clathrin-coated pits driven by epsin". Nature. 419 (6905): 361–366. Bibcode:2002Natur.419..361F. doi:10.1038/nature01020. PMID 12353027. S2CID 4372368.
  • Fotin A, Cheng Y, Sliz P, Grigorieff N, Harrison SC, Kirchhausen T, et al. (December 2004). "Molecular model for a complete clathrin lattice from electron cryomicroscopy". Nature. 432 (7017): 573–579. Bibcode:2004Natur.432..573F. doi:10.1038/nature03079. PMID 15502812. S2CID 4396282.
  • Mousavi SA, Malerød L, Berg T, Kjeken R (January 2004). "Clathrin-dependent endocytosis". The Biochemical Journal. 377 (Pt 1): 1–16. doi:10.1042/BJ20031000. PMC 1223844. PMID 14505490.
  • Smith CJ, Grigorieff N, Pearse BM (September 1998). "Clathrin coats at 21 A resolution: a cellular assembly designed to recycle multiple membrane receptors". The EMBO Journal. 17 (17): 4943–4953. doi:10.1093/emboj/17.17.4943. PMC 1170823. PMID 9724631. (Model of Clathrin assembly)
  • Pérez-Gómez J, Moore I (March 2007). "Plant endocytosis: it is clathrin after all". Current Biology. 17 (6): R217–R219. Bibcode:2007CBio...17.R217P. doi:10.1016/j.cub.2007.01.045. PMID 17371763. S2CID 17680351. (Review on involvement of clathrin in plant endocytosis)
  • Royle SJ, Bright NA, Lagnado L (April 2005). "Clathrin is required for the function of the mitotic spindle". Nature. 434 (7037): 1152–1157. Bibcode:2005Natur.434.1152R. doi:10.1038/nature03502. PMC 3492753. PMID 15858577.
  • Hood FE, Williams SJ, Burgess SG, Richards MW, Roth D, Straube A, et al. (August 2013). "Coordination of adjacent domains mediates TACC3-ch-TOG-clathrin assembly and mitotic spindle binding". The Journal of Cell Biology. 202 (3): 463–478. doi:10.1083/jcb.201211127. PMC 3734082. PMID 23918938.
  • Knuehl C, Chen CY, Manalo V, Hwang PK, Ota N, Brodsky FM (December 2006). "Novel binding sites on clathrin and adaptors regulate distinct aspects of coat assembly". Traffic. 7 (12): 1688–1700. doi:10.1111/j.1600-0854.2006.00499.x. PMID 17052248. S2CID 19087208.
  • Edeling MA, Smith C, Owen D (January 2006). "Life of a clathrin coat: insights from clathrin and AP structures". Nature Reviews. Molecular Cell Biology. 7 (1): 32–44. doi:10.1038/nrm1786. PMID 16493411. S2CID 19393938.
  • Dutta D, Williamson CD, Cole NB, Donaldson JG (Sep 2012). "Pitstop 2 is a potent inhibitor of clathrin-independent endocytosis". PLOS ONE. 7 (9): e45799. Bibcode:2012PLoSO...745799D. doi:10.1371/journal.pone.0045799. PMC 3448704. PMID 23029248.

External links edit

April 08, 2024
clathrin, protein, that, plays, major, role, formation, coated, vesicles, first, isolated, barbara, pearse, 1976, forms, triskelion, shape, composed, three, clathrin, heavy, chains, three, light, chains, when, triskelia, interact, they, form, polyhedral, latti. Clathrin is a protein that plays a major role in the formation of coated vesicles Clathrin was first isolated by Barbara Pearse in 1976 1 It forms a triskelion shape composed of three clathrin heavy chains and three light chains When the triskelia interact they form a polyhedral lattice that surrounds the vesicle The protein s name refers to this lattice structure deriving from Latin clathri meaning lattice 2 Barbara Pearse named the protein clathrin at the suggestion of Graeme Mitchison selecting it from three possible options 3 Coat proteins like clathrin are used to build small vesicles in order to transport molecules within cells The endocytosis and exocytosis of vesicles allows cells to communicate to transfer nutrients to import signaling receptors to mediate an immune response after sampling the extracellular world and to clean up the cell debris left by tissue inflammation The endocytic pathway can be hijacked by viruses and other pathogens in order to gain entry to the cell during infection 4 Clathrin heavy N terminal propeller repeatClathrin terminal domainIdentifiersSymbolClathrin propelPfamPF01394Pfam clanCL0020InterProIPR022365SCOP21bpo SCOPe SUPFAMAvailable protein structures Pfam structures ECOD PDBRCSB PDB PDBe PDBjPDBsumstructure summaryClathrin heavy chain linkerclathrin heavy chain proximal repeat linker IdentifiersSymbolClathrin linkPfamPF09268Pfam clanCL0020InterProIPR015348SCOP21b89 SCOPe SUPFAMAvailable protein structures Pfam structures ECOD PDBRCSB PDB PDBe PDBjPDBsumstructure summaryCHCR VPS 7 fold repeatIdentifiersSymbolClathrin propelPfamPF00637Pfam clanCL0020InterProIPR000547SMARTSM00299PROSITEPS50236CATH1b89SCOP21b89 SCOPe SUPFAMAvailable protein structures Pfam structures ECOD PDBRCSB PDB PDBe PDBjPDBsumstructure summaryClathrin light chainIdentifiersSymbolClathrin lg chPfamPF01086InterProIPR000996PROSITEPDOC00196SCOP23iyv SCOPe SUPFAMAvailable protein structures Pfam structures ECOD PDBRCSB PDB PDBe PDBjPDBsumstructure summary Contents 1 Structure 2 Function 3 See also 4 References 5 Further reading 6 External linksStructure editClathrin light chain aIdentifiersSymbolCLTANCBI gene1211HGNCCLTA HGNC 2090 CLTA UniProtP09496Other dataLocusChr 9 q13Search forStructuresSwiss modelDomainsInterProClathrin light chain bIdentifiersSymbolCLTBNCBI gene1212HGNC2091OMIM118970RefSeqNM 001834UniProtP09497Other dataLocusChr 5 q35Search forStructuresSwiss modelDomainsInterProClathrin heavy chain 1IdentifiersSymbolCLTCAlt symbolsCHC CHC17 CLTCL2NCBI gene1213HGNC2092OMIM118955RefSeqNM 004859UniProtQ00610Other dataLocusChr 17 q23 1 qterSearch forStructuresSwiss modelDomainsInterProClathrin heavy chain 2IdentifiersSymbolCLTCL1Alt symbolsCLTCLNCBI gene8218HGNC2093OMIM601273RefSeqNM 001835UniProtP53675Other dataLocusChr 22 q11 21Search forStructuresSwiss modelDomainsInterProThe clathrin triskelion is composed of three clathrin heavy chains interacting at their C termini each 190 kDa heavy chain has a 25 kDa light chain tightly bound to it The three heavy chains provide the structural backbone of the clathrin lattice and the three light chains are thought to regulate the formation and disassembly of a clathrin lattice There are two forms of clathrin light chains designated a and b The main clathrin heavy chain located on chromosome 17 in humans is found in all cells A second clathrin heavy chain gene on chromosome 22 is expressed in muscle 5 Clathrin heavy chain is often described as a leg with subdomains representing the foot the N terminal domain followed by the ankle distal leg knee proximal leg and trimerization domains The N terminal domain consists of a seven bladed b propeller structure The other domains form a super helix of short alpha helices This was originally determined from the structure of the proximal leg domain that identified and is composed of a smaller structural module referred to as clathrin heavy chain repeat motifs The light chains bind primarily to the proximal leg portion of the heavy chain with some interaction near the trimerization domain The b propeller at the foot of clathrin contains multiple binding sites for interaction with other proteins 5 nbsp A clathrin cage with a single triskelion highlighted in blue CryoEM map EMD 5119 was rendered in UCSF Chimera and one clathrin triskelion was highlighted nbsp Each cage has 12 pentagons Mini coat left has 4 hexagons and tetrahedral symmetry as in a truncated triakis tetrahedron Hexagonal barrel middle has 8 hexagons and D6 symmetry Soccer ball right has 20 hexagons and icosahedral symmetry as in a truncated icosahedron When triskelia assemble together in solution they can interact with enough flexibility to form 6 sided rings hexagons that yield a flat lattice or 5 sided rings pentagons that are necessary for curved lattice formation When many triskelions connect they can form a basket like structure The structure shown is built of 36 triskelia one of which is shown in blue Another common assembly is a truncated icosahedron To enclose a vesicle exactly 12 pentagons must be present in the lattice In a cell clathrin triskelion in the cytoplasm binds to an adaptor protein that has bound membrane linking one of its three feet to the membrane at a time Clathrin cannot bind to membrane or cargo directly and instead uses adaptor proteins to do this This triskelion will bind to other membrane attached triskelia to form a rounded lattice of hexagons and pentagons reminiscent of the panels on a soccer ball that pulls the membrane into a bud By constructing different combinations of 5 sided and 6 sided rings vesicles of different sizes may assemble The smallest clathrin cage commonly imaged called a mini coat has 12 pentagons and only two hexagons Even smaller cages with zero hexagons probably do not form from the native protein because the feet of the triskelia are too bulky 6 Function edit nbsp Mechanism of clathrin mediated endocytosis Clathrin performs critical roles in shaping rounded vesicles in the cytoplasm for intracellular trafficking Clathrin coated vesicles CCVs selectively sort cargo at the cell membrane trans Golgi network and endosomal compartments for multiple membrane traffic pathways After a vesicle buds into the cytoplasm the coat rapidly disassembles allowing the clathrin to recycle while the vesicle gets transported to a variety of locations Adaptor molecules are responsible for self assembly and recruitment Two examples of adaptor proteins are AP180 7 and epsin 8 9 10 AP180 is used in synaptic vesicle formation It recruits clathrin to membranes and also promotes its polymerization Epsin also recruits clathrin to membranes and promotes its polymerization and can help deform the membrane and thus clathrin coated vesicles can bud In a cell a triskelion floating in the cytoplasm binds to an adaptor protein linking one of its feet to the membrane at a time The triskelion foot will bind to other ones attached to the membrane to form a polyhedral lattice triskelion foot which pulls the membrane into a bud The foot does not bind directly to the membrane but binds to the adaptor proteins that recognize the molecules on the membrane surface Clathrin has another function aside from the coating of organelles In non dividing cells the formation of clathrin coated vesicles occurs continuously Formation of clathrin coated vesicles is shut down in cells undergoing mitosis During mitosis clathrin binds to the spindle apparatus in complex with two other proteins TACC3 and ch TOG CKAP5 Clathrin aids in the congression of chromosomes by stabilizing kinetochore fibers of the mitotic spindle The amino terminal domain of the clathrin heavy chain and the TACC domain of TACC3 make the microtubule binding surface for TACC3 ch TOG clathrin to bind to the mitotic spindle The stabilization of kinetochore fibers requires the trimeric structure of clathrin in order to crosslink microtubules 11 12 13 Clathrin mediated endocytosis CME regulates many cellular physiological processes such as the internalization of growth factors and receptors entry of pathogens and synaptic transmission It is believed that cellular invaders use the nutrient pathway to gain access to a cell s replicating mechanisms Certain signalling molecules open the nutrients pathway 1 Two chemical compounds called Pitstop 1 and Pitstop 2 selective clathrin inhibitors can interfere with the pathogenic activity and thus protect the cells against invasion These two compounds selectively block the endocytic ligand association with the clathrin terminal domain in vitro 14 However the specificity of these compounds to block clathrin mediated endocytosis has been questioned 15 In later studies however the specificity of Pitstop 2 was validated as being clathrin dependent 16 See also editAdaptin Cap formation Cell migration DynaminReferences edit a b Pearse BM April 1976 Clathrin a unique protein associated with intracellular transfer of membrane by coated vesicles Proceedings of the National Academy of Sciences of the United States of America 73 4 1255 1259 Bibcode 1976PNAS 73 1255P doi 10 1073 pnas 73 4 1255 PMC 430241 PMID 1063406 clathrate adjective Merriam Webster Retrieved 29 November 2023 Pearse BM September 1987 Clathrin and coated vesicles EMBO J 6 9 2507 12 doi 10 1002 j 1460 2075 1987 tb02536 x PMC 553666 PMID 2890519 InterPro Archived from the original on 2016 01 16 Retrieved 2015 10 07 a b Robinson MS December 2015 Forty Years of Clathrin coated Vesicles Traffic 16 12 1210 38 doi 10 1111 tra 12335 PMID 26403691 Fotin A Kirchhausen T Grigorieff N Harrison SC Walz T Cheng Y December 2006 Structure determination of clathrin coats to subnanometer resolution by single particle cryo electron microscopy J Struct Biol 156 3 453 60 doi 10 1016 j jsb 2006 07 001 PMC 2910098 PMID 16908193 McMahon HT Clathrin and its interactions with AP180 MRC Laboratory of Molecular Biology Archived from the original on 2009 05 01 Retrieved 2009 04 17 micrographs of clathrin assembly McMahon HT Epsin 1 EM gallery MRC Laboratory of Molecular Biology Archived from the original on 2009 01 02 Retrieved 2009 04 17 micrographs of vesicle budding Ford MG Pearse BM Higgins MK Vallis Y Owen DJ Gibson A et al February 2001 Simultaneous binding of PtdIns 4 5 P2 and clathrin by AP180 in the nucleation of clathrin lattices on membranes PDF Science 291 5506 1051 1055 Bibcode 2001Sci 291 1051F CiteSeerX 10 1 1 407 6006 doi 10 1126 science 291 5506 1051 PMID 11161218 Archived from the original PDF on 2008 11 21 Retrieved 2009 04 17 Higgins MK McMahon HT May 2002 Snap shots of clathrin mediated endocytosis PDF Trends in Biochemical Sciences 27 5 257 263 doi 10 1016 S0968 0004 02 02089 3 PMID 12076538 Archived from the original PDF on 2008 11 21 Retrieved 2009 04 17 Royle SJ Bright NA Lagnado L April 2005 Clathrin is required for the function of the mitotic spindle Nature 434 7037 1152 1157 Bibcode 2005Natur 434 1152R doi 10 1038 nature03502 PMC 3492753 PMID 15858577 Hood FE Williams SJ Burgess SG Richards MW Roth D Straube A et al August 2013 Coordination of adjacent domains mediates TACC3 ch TOG clathrin assembly and mitotic spindle binding The Journal of Cell Biology 202 3 463 478 doi 10 1083 jcb 201211127 PMC 3734082 PMID 23918938 Prichard KL O Brien NS Murcia SR Baker JR McCluskey A 2022 01 18 Role of Clathrin and Dynamin in Clathrin Mediated Endocytosis Synaptic Vesicle Recycling and Implications in Neurological Diseases Frontiers in Cellular Neuroscience 15 754110 doi 10 3389 fncel 2021 754110 PMC 8805674 PMID 35115907 Role of the Clathrin Terminal Domain in Regulating Coated Pit Dynamics Revealed by Small Molecule Inhibition Cell Volume 146 Issue 3 471 484 5 August 2011 Abstract Archived 2012 01 19 at the Wayback Machine Dutta D Williamson CD Cole NB Donaldson JG Sep 2012 Pitstop 2 is a potent inhibitor of clathrin independent endocytosis PLOS ONE 7 9 e45799 Bibcode 2012PLoSO 745799D doi 10 1371 journal pone 0045799 PMC 3448704 PMID 23029248 Robertson MJ Horatscheck A Sauer S von Kleist L Baker JR Stahlschmidt W et al November 2016 5 Aryl 2 naphtha 1 yl sulfonamido thiazol 4 5H ones as clathrin inhibitors Organic amp Biomolecular Chemistry 14 47 11266 11278 doi 10 1039 C6OB02308H PMID 27853797 Further reading editWakeham DE Chen CY Greene B Hwang PK Brodsky FM October 2003 Clathrin self assembly involves coordinated weak interactions favorable for cellular regulation The EMBO Journal 22 19 4980 4990 doi 10 1093 emboj cdg511 PMC 204494 PMID 14517237 Ford MG Mills IG Peter BJ Vallis Y Praefcke GJ Evans PR et al September 2002 Curvature of clathrin coated pits driven by epsin Nature 419 6905 361 366 Bibcode 2002Natur 419 361F doi 10 1038 nature01020 PMID 12353027 S2CID 4372368 Fotin A Cheng Y Sliz P Grigorieff N Harrison SC Kirchhausen T et al December 2004 Molecular model for a complete clathrin lattice from electron cryomicroscopy Nature 432 7017 573 579 Bibcode 2004Natur 432 573F doi 10 1038 nature03079 PMID 15502812 S2CID 4396282 Mousavi SA Malerod L Berg T Kjeken R January 2004 Clathrin dependent endocytosis The Biochemical Journal 377 Pt 1 1 16 doi 10 1042 BJ20031000 PMC 1223844 PMID 14505490 Smith CJ Grigorieff N Pearse BM September 1998 Clathrin coats at 21 A resolution a cellular assembly designed to recycle multiple membrane receptors The EMBO Journal 17 17 4943 4953 doi 10 1093 emboj 17 17 4943 PMC 1170823 PMID 9724631 Model of Clathrin assembly Perez Gomez J Moore I March 2007 Plant endocytosis it is clathrin after all Current Biology 17 6 R217 R219 Bibcode 2007CBio 17 R217P doi 10 1016 j cub 2007 01 045 PMID 17371763 S2CID 17680351 Review on involvement of clathrin in plant endocytosis Royle SJ Bright NA Lagnado L April 2005 Clathrin is required for the function of the mitotic spindle Nature 434 7037 1152 1157 Bibcode 2005Natur 434 1152R doi 10 1038 nature03502 PMC 3492753 PMID 15858577 Hood FE Williams SJ Burgess SG Richards MW Roth D Straube A et al August 2013 Coordination of adjacent domains mediates TACC3 ch TOG clathrin assembly and mitotic spindle binding The Journal of Cell Biology 202 3 463 478 doi 10 1083 jcb 201211127 PMC 3734082 PMID 23918938 Knuehl C Chen CY Manalo V Hwang PK Ota N Brodsky FM December 2006 Novel binding sites on clathrin and adaptors regulate distinct aspects of coat assembly Traffic 7 12 1688 1700 doi 10 1111 j 1600 0854 2006 00499 x PMID 17052248 S2CID 19087208 Edeling MA Smith C Owen D January 2006 Life of a clathrin coat insights from clathrin and AP structures Nature Reviews Molecular Cell Biology 7 1 32 44 doi 10 1038 nrm1786 PMID 16493411 S2CID 19393938 Dutta D Williamson CD Cole NB Donaldson JG Sep 2012 Pitstop 2 is a potent inhibitor of clathrin independent endocytosis PLOS ONE 7 9 e45799 Bibcode 2012PLoSO 745799D doi 10 1371 journal pone 0045799 PMC 3448704 PMID 23029248 External links editMBInfo Clathrin Mediated Endocytosis Eukaryotic Linear Motif resource motif class LIG Clathr ClatBox 1 Eukaryotic Linear Motif resource motif class LIG Clathr ClatBox 2 Clathrin structure Membrane Dynamics Clathrin Dynamics permanent dead link ASCB Image amp Video Library Retrieved from https en wikipedia org w index php title Clathrin amp oldid 1215740188, wikipedia, wiki, book, books, library,

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