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Profilin

April 14, 2024

Profilin is an actin-binding protein involved in the dynamic turnover and reconstruction of the actin cytoskeleton.[1] It is found in most eukaryotic organisms. Profilin is important for spatially and temporally controlled growth of actin microfilaments, which is an essential process in cellular locomotion and cell shape changes. This restructuring of the actin cytoskeleton is essential for processes such as organ development, wound healing, and the hunting down of infectious intruders by cells of the immune system.

Profilin
Profilin (blue) in complex with actin (green). (PDB code: 2BTF​)
Identifiers
SymbolProfilin
PfamPF00235
InterProIPR002097
SMARTPROF
PROSITEPS00414
SCOP22btf / SCOPe / SUPFAM
CDDcd00148
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary
PDB2btf​

Profilin also binds sequences rich in the amino acid proline in diverse proteins. While most profilin in the cell is bound to actin, profilins have over 50 different binding partners. Many of those are related to actin regulation, but profilin also seems to be involved in activities in the nucleus such as mRNA splicing.[2]

Profilin is the major allergen (via IgE) present in birch, grass, and other pollen.[citation needed]

Sources and distribution edit

Profilins are proteins of molecular weights of roughly 14–19 kDa. They are present as single genes in yeast, insects, and worms, and as multiple genes in many other organisms including plants. In mammalian cells, four profilin isoforms have been discovered; profilin-I is expressed in most tissues while profilin-II is predominant in brain and kidney.[3]

Asgard archaea use profilins.[4] Multiple eukaryotic diatom species lack profilins.[5]

Profilin is essential to host cell invasion by Toxoplasma gondii. Toxoplasma profilin is the specific pathogen-associated molecular pattern (PAMP) of TLRs 5, 11, and 12.[6]

Regulation of actin dynamics edit

Profilin enhances actin growth in two ways:

  • Profilin binds to monomeric actin thereby occupying an actin-actin contact site; in effect, profilin sequesters actin from the pool of polymerizable actin monomers. However, profilin also catalyzes the exchange of actin-bound ADP to ATP thereby converting poorly polymerizing ADP-actin monomers into readily polymerizing ATP-actin monomers. On top of that, profilin has a higher affinity for ATP- than for ADP-actin monomers. Thus in a mixture of actin, profilin, and nucleotides (ADP and ATP), actin will polymerize to a certain extent, which may be estimated by the law of mass action.[citation needed]
  • Profilin-actin complexes are fed into growing actin polymers by proteins such as formin, Wiskott-Aldrich syndrome protein and Vasodilator-stimulated phosphoprotein which contain proline-rich FH1-domains. This mode of stimulated actin polymerization is much faster than unaided polymerization. Profilin is essential for this mode of polymerization because it recruits the actin monomers to the proline-rich proteins.[citation needed]

Profilin binds some variants of membrane phospholipids (phosphatidylinositol (4,5)-bisphosphate and inositol trisphosphate). The function of this interaction is the sequestration of profilin in an "inactive" form, from where it can be released by action of the enzyme phospholipase C.[citation needed]

Profilin negatively regulates PI(3,4)P2 limiting recruitment of lamellipodia to the leading edge of the cell.[7]

Profilin is one of the most abundant actin monomer binders, but proteins such as CAP and (in mammals) thymosin β4 have some functional overlaps with profilin. In contrast, ADF/cofilin has some properties that antagonize profilin action.

History of discovery edit

Profilin was first described by Lars Carlsson in the lab of Uno Lindberg and co-workers in the early 1970s as the first actin monomer binding protein.[8] It followed the realization that not only muscle, but also non-muscle cells, contained high concentrations of actin, albeit in part in an unpolymerized form. Profilin was then believed to sequester actin monomers (keep them in a pro-filamentous form), and release them upon a signal to make them accessible for fast actin polymer growth.

Allergen edit

Profilin allergy is significantly associated with respiratory allergy to grass pollen ( hay fever). After a person first becomes allergic to profilin through inhalation of grass or tree pollen, allergy to profilin-containing food and development of pollen-food syndrome occurs [9]: 3  How often pollen-allergic people across Europe become profilin allergic varies widely; As of 1997, from about 5% of Swedish birch pollen–allergic people to 51% in Spanish people allergic to Mercurialis annua were profilin allergic.[9] Profilin is the major allergen of certain food plants, for example, melon, orange, and soybean and thus allergy to melon, citrus fruits, tomato, and banana is a clinical marker of profilin hypersensitivity.[9] As of 2018 there was no "solid therapeutic approach" to treat profilin allergy.[9]

As of 2018, the list of members of the profilin family identified as allergens contained:[9]

Human genes edit

References edit

  1. ^ Gunning PW, Ghoshdastider U, Whitaker S, Popp D, Robinson RC (June 2015). "The evolution of compositionally and functionally distinct actin filaments". Journal of Cell Science. 128 (11): 2009–19. doi:10.1242/jcs.165563. PMID 25788699.
  2. ^ Di Nardo A, Gareus R, Kwiatkowski D, Witke W (November 2000). "Alternative splicing of the mouse profilin II gene generates functionally different profilin isoforms" (PDF). Journal of Cell Science. 113 (Pt 21): 3795–803. doi:10.1242/jcs.113.21.3795. PMID 11034907.
  3. ^ Witke W, Podtelejnikov AV, Di Nardo A, Sutherland JD, Gurniak CB, Dotti C, Mann M (February 1998). "In mouse brain profilin I and profilin II associate with regulators of the endocytic pathway and actin assembly". The EMBO Journal. 17 (4): 967–76. doi:10.1093/emboj/17.4.967. PMC 1170446. PMID 9463375.
  4. ^ Akıl C, Robinson RC (October 2018). "Genomes of Asgard archaea encode profilins that regulate actin". Nature. 562 (7727): 439–443. Bibcode:2018Natur.562..439A. doi:10.1038/s41586-018-0548-6. PMID 30283132. S2CID 52917038.
  5. ^ Aumeier, Charlotte; Polinski, Ellen; Menzel, Diedrik (October 2015). "Actin, actin-related proteins and profilin in diatoms: a comparative genomic analysis". Marine Genomics. 23: 133–142. doi:10.1016/j.margen.2015.07.002. ISSN 1876-7478. PMID 26298820.
  6. ^ Salazar Gonzalez RM, Shehata H, O'Connell MJ, Yang Y, Moreno-Fernandez ME, Chougnet CA, Aliberti J (August 2014). "Toxoplasma gondii- derived profilin triggers human toll-like receptor 5-dependent cytokine production". Journal of Innate Immunity. 6 (5): 685–94. doi:10.1159/000362367. PMC 4141014. PMID 24861338.
  7. ^ Bae YH, Ding Z, Das T, Wells A, Gertler F, Roy P (December 2010). "Profilin1 regulates PI(3,4)P2 and lamellipodin accumulation at the leading edge thus influencing motility of MDA-MB-231 cells". Proceedings of the National Academy of Sciences of the United States of America. 107 (50): 21547–52. Bibcode:2010PNAS..10721547B. doi:10.1073/pnas.1002309107. PMC 3003040. PMID 21115820.
  8. ^ Carlsson L, Nyström LE, Sundkvist I, Markey F, Lindberg U (September 1977). "Actin polymerizability is influenced by profilin, a low molecular weight protein in non-muscle cells". Journal of Molecular Biology. 115 (3): 465–83. doi:10.1016/0022-2836(77)90166-8. PMID 563468.
  9. ^ a b c d e Rodríguez del Río, P; Díaz-Perales, A; Sánchez-García, S; Escudero, C; Ibáñez, Md; Méndez-Brea, P; Barber, D (2018-02-19). "Profilin, a Change in the Paradigm". Journal of Investigational Allergology and Clinical Immunology. 28 (1): 1–12. doi:10.18176/jiaci.0193. PMID 28760720.

Further reading edit

Bae YH, Ding Z, Das T, Wells A, Gertler F, Roy P (December 2010). "Profilin1 regulates PI(3,4)P2 and lamellipodin accumulation at the leading edge thus influencing motility of MDA-MB-231 cells". Proceedings of the National Academy of Sciences of the United States of America. 107 (50): 21547–52. Bibcode:2010PNAS..10721547B. doi:10.1073/pnas.1002309107. PMC 3003040. PMID 21115820.

External links edit

April 14, 2024
profilin, actin, binding, protein, involved, dynamic, turnover, reconstruction, actin, cytoskeleton, found, most, eukaryotic, organisms, important, spatially, temporally, controlled, growth, actin, microfilaments, which, essential, process, cellular, locomotio. Profilin is an actin binding protein involved in the dynamic turnover and reconstruction of the actin cytoskeleton 1 It is found in most eukaryotic organisms Profilin is important for spatially and temporally controlled growth of actin microfilaments which is an essential process in cellular locomotion and cell shape changes This restructuring of the actin cytoskeleton is essential for processes such as organ development wound healing and the hunting down of infectious intruders by cells of the immune system ProfilinProfilin blue in complex with actin green PDB code 2BTF IdentifiersSymbolProfilinPfamPF00235InterProIPR002097SMARTPROFPROSITEPS00414SCOP22btf SCOPe SUPFAMCDDcd00148Available protein structures Pfam structures ECOD PDBRCSB PDB PDBe PDBjPDBsumstructure summaryPDB2btf Profilin also binds sequences rich in the amino acid proline in diverse proteins While most profilin in the cell is bound to actin profilins have over 50 different binding partners Many of those are related to actin regulation but profilin also seems to be involved in activities in the nucleus such as mRNA splicing 2 Profilin is the major allergen via IgE present in birch grass and other pollen citation needed Contents 1 Sources and distribution 2 Regulation of actin dynamics 3 History of discovery 4 Allergen 5 Human genes 6 References 7 Further reading 8 External linksSources and distribution editProfilins are proteins of molecular weights of roughly 14 19 kDa They are present as single genes in yeast insects and worms and as multiple genes in many other organisms including plants In mammalian cells four profilin isoforms have been discovered profilin I is expressed in most tissues while profilin II is predominant in brain and kidney 3 Asgard archaea use profilins 4 Multiple eukaryotic diatom species lack profilins 5 Profilin is essential to host cell invasion by Toxoplasma gondii Toxoplasma profilin is the specific pathogen associated molecular pattern PAMP of TLRs 5 11 and 12 6 Regulation of actin dynamics editProfilin enhances actin growth in two ways Profilin binds to monomeric actin thereby occupying an actin actin contact site in effect profilin sequesters actin from the pool of polymerizable actin monomers However profilin also catalyzes the exchange of actin bound ADP to ATP thereby converting poorly polymerizing ADP actin monomers into readily polymerizing ATP actin monomers On top of that profilin has a higher affinity for ATP than for ADP actin monomers Thus in a mixture of actin profilin and nucleotides ADP and ATP actin will polymerize to a certain extent which may be estimated by the law of mass action citation needed Profilin actin complexes are fed into growing actin polymers by proteins such as formin Wiskott Aldrich syndrome protein and Vasodilator stimulated phosphoprotein which contain proline rich FH1 domains This mode of stimulated actin polymerization is much faster than unaided polymerization Profilin is essential for this mode of polymerization because it recruits the actin monomers to the proline rich proteins citation needed Profilin binds some variants of membrane phospholipids phosphatidylinositol 4 5 bisphosphate and inositol trisphosphate The function of this interaction is the sequestration of profilin in an inactive form from where it can be released by action of the enzyme phospholipase C citation needed Profilin negatively regulates PI 3 4 P2 limiting recruitment of lamellipodia to the leading edge of the cell 7 Profilin is one of the most abundant actin monomer binders but proteins such as CAP and in mammals thymosin b4 have some functional overlaps with profilin In contrast ADF cofilin has some properties that antagonize profilin action History of discovery editProfilin was first described by Lars Carlsson in the lab of Uno Lindberg and co workers in the early 1970s as the first actin monomer binding protein 8 It followed the realization that not only muscle but also non muscle cells contained high concentrations of actin albeit in part in an unpolymerized form Profilin was then believed to sequester actin monomers keep them in a pro filamentous form and release them upon a signal to make them accessible for fast actin polymer growth Allergen editProfilin allergy is significantly associated with respiratory allergy to grass pollen hay fever After a person first becomes allergic to profilin through inhalation of grass or tree pollen allergy to profilin containing food and development of pollen food syndrome occurs 9 3 How often pollen allergic people across Europe become profilin allergic varies widely As of 1997 from about 5 of Swedish birch pollen allergic people to 51 in Spanish people allergic to Mercurialis annua were profilin allergic 9 Profilin is the major allergen of certain food plants for example melon orange and soybean and thus allergy to melon citrus fruits tomato and banana is a clinical marker of profilin hypersensitivity 9 As of 2018 there was no solid therapeutic approach to treat profilin allergy 9 As of 2018 the list of members of the profilin family identified as allergens contained 9 Actinidia deliciosa kiwi fruit Ambrosia artemisiifolia short ragweed Ananas comosus pineapple Apium graveolens celery Arachis hypogaea peanut Artemisia vulgaris mugwort Betula verrucosa European white birch and Betula pendula silver birch Capsicum annuum bell pepper Chenopodium album pigweed Citrus sinensis sweet orange Corylus avellana hazel Cucumis melo muskmelon Daucus carota carrot Glycine max soybean Helianthus annuus sunflower Hevea brasiliensis para rubber tree latex Malus domestica apple Olea europaea olive Phleum pratense timothy grass Phoenix dactylifera date palm Prunus persica peach Pyrus communis pear Salsola kali Russian thistle Sinapis alba yellow mustard Solanum lycopersicum tomato Human genes editPFN1 PFN2 PFN3 PFN4 PFN5References edit Gunning PW Ghoshdastider U Whitaker S Popp D Robinson RC June 2015 The evolution of compositionally and functionally distinct actin filaments Journal of Cell Science 128 11 2009 19 doi 10 1242 jcs 165563 PMID 25788699 Di Nardo A Gareus R Kwiatkowski D Witke W November 2000 Alternative splicing of the mouse profilin II gene generates functionally different profilin isoforms PDF Journal of Cell Science 113 Pt 21 3795 803 doi 10 1242 jcs 113 21 3795 PMID 11034907 Witke W Podtelejnikov AV Di Nardo A Sutherland JD Gurniak CB Dotti C Mann M February 1998 In mouse brain profilin I and profilin II associate with regulators of the endocytic pathway and actin assembly The EMBO Journal 17 4 967 76 doi 10 1093 emboj 17 4 967 PMC 1170446 PMID 9463375 Akil C Robinson RC October 2018 Genomes of Asgard archaea encode profilins that regulate actin Nature 562 7727 439 443 Bibcode 2018Natur 562 439A doi 10 1038 s41586 018 0548 6 PMID 30283132 S2CID 52917038 Aumeier Charlotte Polinski Ellen Menzel Diedrik October 2015 Actin actin related proteins and profilin in diatoms a comparative genomic analysis Marine Genomics 23 133 142 doi 10 1016 j margen 2015 07 002 ISSN 1876 7478 PMID 26298820 Salazar Gonzalez RM Shehata H O Connell MJ Yang Y Moreno Fernandez ME Chougnet CA Aliberti J August 2014 Toxoplasma gondii derived profilin triggers human toll like receptor 5 dependent cytokine production Journal of Innate Immunity 6 5 685 94 doi 10 1159 000362367 PMC 4141014 PMID 24861338 Bae YH Ding Z Das T Wells A Gertler F Roy P December 2010 Profilin1 regulates PI 3 4 P2 and lamellipodin accumulation at the leading edge thus influencing motility of MDA MB 231 cells Proceedings of the National Academy of Sciences of the United States of America 107 50 21547 52 Bibcode 2010PNAS 10721547B doi 10 1073 pnas 1002309107 PMC 3003040 PMID 21115820 Carlsson L Nystrom LE Sundkvist I Markey F Lindberg U September 1977 Actin polymerizability is influenced by profilin a low molecular weight protein in non muscle cells Journal of Molecular Biology 115 3 465 83 doi 10 1016 0022 2836 77 90166 8 PMID 563468 a b c d e Rodriguez del Rio P Diaz Perales A Sanchez Garcia S Escudero C Ibanez Md Mendez Brea P Barber D 2018 02 19 Profilin a Change in the Paradigm Journal of Investigational Allergology and Clinical Immunology 28 1 1 12 doi 10 18176 jiaci 0193 PMID 28760720 Further reading editBae YH Ding Z Das T Wells A Gertler F Roy P December 2010 Profilin1 regulates PI 3 4 P2 and lamellipodin accumulation at the leading edge thus influencing motility of MDA MB 231 cells Proceedings of the National Academy of Sciences of the United States of America 107 50 21547 52 Bibcode 2010PNAS 10721547B doi 10 1073 pnas 1002309107 PMC 3003040 PMID 21115820 External links editProfilins at the U S National Library of Medicine Medical Subject Headings MeSH Retrieved from https en wikipedia org w index php title Profilin amp oldid 1187730305, wikipedia, wiki, book, books, library,

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