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Inositol trisphosphate receptor

January 20, 2023

See also: Ryanodine-Inositol 1,4,5-triphosphate receptor calcium channels

Inositol trisphosphate receptor (InsP3R) is a membrane glycoprotein complex acting as a Ca2+ channel activated by inositol trisphosphate (InsP3). InsP3R is very diverse among organisms, and is necessary for the control of cellular and physiological processes including cell division, cell proliferation, apoptosis, fertilization, development, behavior, learning and memory.[2] Inositol triphosphate receptor represents a dominant second messenger leading to the release of Ca2+ from intracellular store sites. There is strong evidence suggesting that the InsP3R plays an important role in the conversion of external stimuli to intracellular Ca2+ signals characterized by complex patterns relative to both space and time, such as Ca2+ waves and oscillations.[3]

inositol 1,4,5-trisphosphate receptor, type 1[1]
Crystal structure of the ligand binding suppressor domain of type 1 inositol 1,4,5-trisphosphate receptor
Identifiers
SymbolITPR1
NCBI gene3708
HGNC6180
OMIM147265
RefSeqNM_002222
UniProtQ14643
Other data
LocusChr. 3 p26.1
Search for
StructuresSwiss-model
DomainsInterPro
inositol 1,4,5-trisphosphate receptor, type 2
Identifiers
SymbolITPR2
NCBI gene3709
HGNCstructure of the ligand binding suppressor domain of type 1 inositol 1,4,5-trisphosphate receptor 6181 Crystal structure of the ligand binding suppressor domain of type 1 inositol 1,4,5-trisphosphate receptor 6181
OMIM600144
RefSeqNM_002223
UniProtQ14571
Other data
LocusChr. 12 p11.23
Search for
StructuresSwiss-model
DomainsInterPro
inositol 1,4,5-trisphosphate receptor, type 3
Single-particle cryo-EM structure of the IP3-bound resting state.
Identifiers
SymbolITPR3
NCBI gene3710
HGNC6182
OMIM147267
RefSeqNM_002224
UniProtQ14573
Other data
LocusChr. 6 p21.31
Search for
StructuresSwiss-model
DomainsInterPro

Discovery

The InsP3 receptor was first purified from rat cerebellum by neuroscientists Surachai Supattapone and Solomon Snyder at Johns Hopkins University School of Medicine.[4]

The cDNA of the InsP3 receptor was first cloned in the laboratory of Katsuhiko Mikoshiba. The initial sequencing was reported as an unknown protein enriched in the cerebellum called P400.[5] The large size of this open reading frame indicated a molecular weight similar to the protein purified biochemically, and soon thereafter it was confirmed that the protein p400 was in fact the inositol trisphosphate receptor.[6]

Distribution

The receptor has a broad tissue distribution but is especially abundant in the cerebellum. Most of the InsP3Rs are found integrated into the endoplasmic reticulum.

Structure

Several X-ray crystallographic [7][8][9] and electron cryomicroscopic (cryo-EM) [10][11][12][13][14][15][16] structures of IP3Rs from mouse, rat, and human have defined the overall architecture of the channel. The 1.2 MDa C4-symmetric assembly consists of an ER-embedded transmembrane domain (TMD) in a domain-swapped 6 transmembrane (6TM) cation channel fold that is capped by a large cytosolic domain (CD). In this manner, IP3Rs share significant homology with the much larger and distantly-related RyRs.[17] The CD contains all known ligand binding sites, including the IP3 binding site, two Ca2+ binding sites, an adenine nucleotide binding site, and a C2H2 Zn2+ finger fold. A comprehensive Ca2+-dependent conformational landscape has recently been defined by cryo-EM.[18]

See also

References

  1. ^ Bosanac I, Yamazaki H, Matsu-Ura T, Michikawa T, Mikoshiba K, Ikura M (January 2005). "Crystal structure of the ligand binding suppressor domain of type 1 inositol 1,4,5-trisphosphate receptor". Molecular Cell. 17 (2): 193–203. doi:10.1016/j.molcel.2004.11.047. PMID 15664189.
  2. ^ Bosanac I, Alattia JR, Mal TK, Chan J, Talarico S, Tong FK, et al. (December 2002). "Structure of the inositol 1,4,5-trisphosphate receptor binding core in complex with its ligand". Nature. 420 (6916): 696–700. Bibcode:2002Natur.420..696B. doi:10.1038/nature01268. PMID 12442173. S2CID 4422308.
  3. ^ Yoshida Y, Imai S (June 1997). "Structure and function of inositol 1,4,5-trisphosphate receptor". Japanese Journal of Pharmacology. 74 (2): 125–137. doi:10.1254/jjp.74.125. PMID 9243320.
  4. ^ Supattapone S, Worley PF, Baraban JM, Snyder SH (January 1988). "Solubilization, purification, and characterization of an inositol trisphosphate receptor". The Journal of Biological Chemistry. 263 (3): 1530–1534. doi:10.1016/S0021-9258(19)57336-7. PMID 2826483.
  5. ^ Furuichi T, Yoshikawa S, Mikoshiba K (July 1989). "Nucleotide sequence of cDNA encoding P400 protein in the mouse cerebellum". Nucleic Acids Research. 17 (13): 5385–5386. doi:10.1093/nar/17.13.5385. PMC 318125. PMID 2762133.
  6. ^ Furuichi T, Yoshikawa S, Miyawaki A, Wada K, Maeda N, Mikoshiba K (November 1989). "Primary structure and functional expression of the inositol 1,4,5-trisphosphate-binding protein P400". Nature. 342 (6245): 32–38. Bibcode:1989Natur.342...32F. doi:10.1038/342032a0. PMID 2554142. S2CID 1781700.
  7. ^ Bosanac I, Alattia JR, Mal TK, Chan J, Talarico S, Tong FK, et al. (December 2002). "Structure of the inositol 1,4,5-trisphosphate receptor binding core in complex with its ligand". Nature. 420 (6916): 696–700. Bibcode:2002Natur.420..696B. doi:10.1038/nature01268. PMID 12442173. S2CID 4422308.
  8. ^ Lin CC, Baek K, Lu Z (September 2011). "Apo and InsP₃-bound crystal structures of the ligand-binding domain of an InsP₃ receptor". Nature Structural & Molecular Biology. 18 (10): 1172–1174. doi:10.1038/nsmb.2112. PMC 3242432. PMID 21892169.
  9. ^ Seo MD, Velamakanni S, Ishiyama N, Stathopulos PB, Rossi AM, Khan SA, et al. (January 2012). "Structural and functional conservation of key domains in InsP3 and ryanodine receptors". Nature. 483 (7387): 108–112. Bibcode:2012Natur.483..108S. doi:10.1038/nature10751. PMC 3378505. PMID 22286060.
  10. ^ Fan G, Baker ML, Wang Z, Baker MR, Sinyagovskiy PA, Chiu W, et al. (November 2015). "Gating machinery of InsP3R channels revealed by electron cryomicroscopy". Nature. 527 (7578): 336–341. Bibcode:2015Natur.527..336F. doi:10.1038/nature15249. PMC 4804758. PMID 26458101.
  11. ^ Paknejad N, Hite RK (August 2018). "Structural basis for the regulation of inositol trisphosphate receptors by Ca2+ and IP3". Nature Structural & Molecular Biology. 25 (8): 660–668. doi:10.1038/s41594-018-0089-6. PMC 6082148. PMID 30013099.
  12. ^ Fan G, Baker MR, Wang Z, Seryshev AB, Ludtke SJ, Baker ML, Serysheva II (December 2018). "Cryo-EM reveals ligand induced allostery underlying InsP3R channel gating". Cell Research. 28 (12): 1158–1170. doi:10.1038/s41422-018-0108-5. PMC 6274648. PMID 30470765.
  13. ^ Azumaya CM, Linton EA, Risener CJ, Nakagawa T, Karakas E (February 2020). "Cryo-EM structure of human type-3 inositol triphosphate receptor reveals the presence of a self-binding peptide that acts as an antagonist". The Journal of Biological Chemistry. 295 (6): 1743–1753. doi:10.1074/jbc.RA119.011570. PMC 7008357. PMID 31915246.
  14. ^ Baker MR, Fan G, Seryshev AB, Agosto MA, Baker ML, Serysheva II (May 2021). "Cryo-EM structure of type 1 IP3R channel in a lipid bilayer". Communications Biology. 4 (1): 625. doi:10.1038/s42003-021-02156-4. PMC 8149723. PMID 34035440.
  15. ^ Schmitz EA, Takahashi H, Karakas E (March 2022). "Structural basis for activation and gating of IP3 receptors". Nature Communications. 13 (1): 1408. Bibcode:2022NatCo..13.1408S. doi:10.1038/s41467-022-29073-2. PMC 8930994. PMID 35301323.
  16. ^ Fan G, Baker MR, Terry LE, Arige V, Chen M, Seryshev AB, et al. (November 2022). "Conformational motions and ligand-binding underlying gating and regulation in IP3R channel". Nature Communications. 13 (1): 6942. Bibcode:2022NatCo..13.6942F. doi:10.1038/s41467-022-34574-1. PMC 9663519. PMID 36376291.
  17. ^ Woll KA, Van Petegem F (January 2022). "Calcium-release channels: structure and function of IP3 receptors and ryanodine receptors". Physiological Reviews. 102 (1): 209–268. doi:10.1152/physrev.00033.2020. PMID 34280054. S2CID 236141016.
  18. ^ Paknejad N, Sapuru V, Hite RK (2022-12-30). "Structural titration reveals Ca2+-dependent conformational landscape of the IP3receptor". bioRxiv. doi:10.1101/2022.12.29.522241. S2CID 255373875.

External links

January 20, 2023
inositol, trisphosphate, receptor, also, ryanodine, inositol, triphosphate, receptor, calcium, channels, insp3r, membrane, glycoprotein, complex, acting, channel, activated, inositol, trisphosphate, insp3, insp3r, very, diverse, among, organisms, necessary, co. See also Ryanodine Inositol 1 4 5 triphosphate receptor calcium channels Inositol trisphosphate receptor InsP3R is a membrane glycoprotein complex acting as a Ca2 channel activated by inositol trisphosphate InsP3 InsP3R is very diverse among organisms and is necessary for the control of cellular and physiological processes including cell division cell proliferation apoptosis fertilization development behavior learning and memory 2 Inositol triphosphate receptor represents a dominant second messenger leading to the release of Ca2 from intracellular store sites There is strong evidence suggesting that the InsP3R plays an important role in the conversion of external stimuli to intracellular Ca2 signals characterized by complex patterns relative to both space and time such as Ca2 waves and oscillations 3 inositol 1 4 5 trisphosphate receptor type 1 1 Crystal structure of the ligand binding suppressor domain of type 1 inositol 1 4 5 trisphosphate receptorIdentifiersSymbolITPR1NCBI gene3708HGNC6180OMIM147265RefSeqNM 002222UniProtQ14643Other dataLocusChr 3 p26 1Search forStructuresSwiss modelDomainsInterProinositol 1 4 5 trisphosphate receptor type 2IdentifiersSymbolITPR2NCBI gene3709HGNCstructure of the ligand binding suppressor domain of type 1 inositol 1 4 5 trisphosphate receptor 6181 Crystal structure of the ligand binding suppressor domain of type 1 inositol 1 4 5 trisphosphate receptor 6181OMIM600144RefSeqNM 002223UniProtQ14571Other dataLocusChr 12 p11 23Search forStructuresSwiss modelDomainsInterProinositol 1 4 5 trisphosphate receptor type 3Single particle cryo EM structure of the IP3 bound resting state IdentifiersSymbolITPR3NCBI gene3710HGNC6182OMIM147267RefSeqNM 002224UniProtQ14573Other dataLocusChr 6 p21 31Search forStructuresSwiss modelDomainsInterPro Contents 1 Discovery 2 Distribution 3 Structure 4 See also 5 References 6 External linksDiscovery EditThe InsP3 receptor was first purified from rat cerebellum by neuroscientists Surachai Supattapone and Solomon Snyder at Johns Hopkins University School of Medicine 4 The cDNA of the InsP3 receptor was first cloned in the laboratory of Katsuhiko Mikoshiba The initial sequencing was reported as an unknown protein enriched in the cerebellum called P400 5 The large size of this open reading frame indicated a molecular weight similar to the protein purified biochemically and soon thereafter it was confirmed that the protein p400 was in fact the inositol trisphosphate receptor 6 Distribution EditThe receptor has a broad tissue distribution but is especially abundant in the cerebellum Most of the InsP3Rs are found integrated into the endoplasmic reticulum Structure EditSeveral X ray crystallographic 7 8 9 and electron cryomicroscopic cryo EM 10 11 12 13 14 15 16 structures of IP3Rs from mouse rat and human have defined the overall architecture of the channel The 1 2 MDa C4 symmetric assembly consists of an ER embedded transmembrane domain TMD in a domain swapped 6 transmembrane 6TM cation channel fold that is capped by a large cytosolic domain CD In this manner IP3Rs share significant homology with the much larger and distantly related RyRs 17 The CD contains all known ligand binding sites including the IP3 binding site two Ca2 binding sites an adenine nucleotide binding site and a C2H2 Zn2 finger fold A comprehensive Ca2 dependent conformational landscape has recently been defined by cryo EM 18 See also EditInositol Inositol phosphate Inositol monophosphate Inositol trisphosphate Inositol pentakisphosphate Inositol hexaphosphate MRVI1 associated through complex formation References Edit Bosanac I Yamazaki H Matsu Ura T Michikawa T Mikoshiba K Ikura M January 2005 Crystal structure of the ligand binding suppressor domain of type 1 inositol 1 4 5 trisphosphate receptor Molecular Cell 17 2 193 203 doi 10 1016 j molcel 2004 11 047 PMID 15664189 Bosanac I Alattia JR Mal TK Chan J Talarico S Tong FK et al December 2002 Structure of the inositol 1 4 5 trisphosphate receptor binding core in complex with its ligand Nature 420 6916 696 700 Bibcode 2002Natur 420 696B doi 10 1038 nature01268 PMID 12442173 S2CID 4422308 Yoshida Y Imai S June 1997 Structure and function of inositol 1 4 5 trisphosphate receptor Japanese Journal of Pharmacology 74 2 125 137 doi 10 1254 jjp 74 125 PMID 9243320 Supattapone S Worley PF Baraban JM Snyder SH January 1988 Solubilization purification and characterization of an inositol trisphosphate receptor The Journal of Biological Chemistry 263 3 1530 1534 doi 10 1016 S0021 9258 19 57336 7 PMID 2826483 Furuichi T Yoshikawa S Mikoshiba K July 1989 Nucleotide sequence of cDNA encoding P400 protein in the mouse cerebellum Nucleic Acids Research 17 13 5385 5386 doi 10 1093 nar 17 13 5385 PMC 318125 PMID 2762133 Furuichi T Yoshikawa S Miyawaki A Wada K Maeda N Mikoshiba K November 1989 Primary structure and functional expression of the inositol 1 4 5 trisphosphate binding protein P400 Nature 342 6245 32 38 Bibcode 1989Natur 342 32F doi 10 1038 342032a0 PMID 2554142 S2CID 1781700 Bosanac I Alattia JR Mal TK Chan J Talarico S Tong FK et al December 2002 Structure of the inositol 1 4 5 trisphosphate receptor binding core in complex with its ligand Nature 420 6916 696 700 Bibcode 2002Natur 420 696B doi 10 1038 nature01268 PMID 12442173 S2CID 4422308 Lin CC Baek K Lu Z September 2011 Apo and InsP bound crystal structures of the ligand binding domain of an InsP receptor Nature Structural amp Molecular Biology 18 10 1172 1174 doi 10 1038 nsmb 2112 PMC 3242432 PMID 21892169 Seo MD Velamakanni S Ishiyama N Stathopulos PB Rossi AM Khan SA et al January 2012 Structural and functional conservation of key domains in InsP3 and ryanodine receptors Nature 483 7387 108 112 Bibcode 2012Natur 483 108S doi 10 1038 nature10751 PMC 3378505 PMID 22286060 Fan G Baker ML Wang Z Baker MR Sinyagovskiy PA Chiu W et al November 2015 Gating machinery of InsP3R channels revealed by electron cryomicroscopy Nature 527 7578 336 341 Bibcode 2015Natur 527 336F doi 10 1038 nature15249 PMC 4804758 PMID 26458101 Paknejad N Hite RK August 2018 Structural basis for the regulation of inositol trisphosphate receptors by Ca2 and IP3 Nature Structural amp Molecular Biology 25 8 660 668 doi 10 1038 s41594 018 0089 6 PMC 6082148 PMID 30013099 Fan G Baker MR Wang Z Seryshev AB Ludtke SJ Baker ML Serysheva II December 2018 Cryo EM reveals ligand induced allostery underlying InsP3R channel gating Cell Research 28 12 1158 1170 doi 10 1038 s41422 018 0108 5 PMC 6274648 PMID 30470765 Azumaya CM Linton EA Risener CJ Nakagawa T Karakas E February 2020 Cryo EM structure of human type 3 inositol triphosphate receptor reveals the presence of a self binding peptide that acts as an antagonist The Journal of Biological Chemistry 295 6 1743 1753 doi 10 1074 jbc RA119 011570 PMC 7008357 PMID 31915246 Baker MR Fan G Seryshev AB Agosto MA Baker ML Serysheva II May 2021 Cryo EM structure of type 1 IP3R channel in a lipid bilayer Communications Biology 4 1 625 doi 10 1038 s42003 021 02156 4 PMC 8149723 PMID 34035440 Schmitz EA Takahashi H Karakas E March 2022 Structural basis for activation and gating of IP3 receptors Nature Communications 13 1 1408 Bibcode 2022NatCo 13 1408S doi 10 1038 s41467 022 29073 2 PMC 8930994 PMID 35301323 Fan G Baker MR Terry LE Arige V Chen M Seryshev AB et al November 2022 Conformational motions and ligand binding underlying gating and regulation in IP3R channel Nature Communications 13 1 6942 Bibcode 2022NatCo 13 6942F doi 10 1038 s41467 022 34574 1 PMC 9663519 PMID 36376291 Woll KA Van Petegem F January 2022 Calcium release channels structure and function of IP3 receptors and ryanodine receptors Physiological Reviews 102 1 209 268 doi 10 1152 physrev 00033 2020 PMID 34280054 S2CID 236141016 Paknejad N Sapuru V Hite RK 2022 12 30 Structural titration reveals Ca2 dependent conformational landscape of the IP3receptor bioRxiv doi 10 1101 2022 12 29 522241 S2CID 255373875 External links EditInositol Trisphosphate Receptor at the US National Library of Medicine Medical Subject Headings MeSH Retrieved from https en wikipedia org w index php title Inositol trisphosphate receptor amp oldid 1133746575, wikipedia, wiki, book, books, library,

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