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Tytuł:
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Non-inositol 1,4,5-trisphosphate (IP 3 ) receptor IP 3 -binding proteins.
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Autorzy:
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Mackrill JJ; Department of Physiology, University College Cork, Western Gateway Building, Western Road, Cork T12 XF62, Ireland. Electronic address: .
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Źródło:
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Biochimica et biophysica acta. Molecular cell research [Biochim Biophys Acta Mol Cell Res] 2023 Jun; Vol. 1870 (5), pp. 119470. Date of Electronic Publication: 2023 Apr 01.
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Typ publikacji:
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Journal Article; Research Support, Non-U.S. Gov't
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Język:
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English
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Imprint Name(s):
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Original Publication: Amsterdam : Elsevier
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MeSH Terms:
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Carrier Proteins*/metabolism
Inositol*
Inositol 1,4,5-Trisphosphate Receptors/metabolism ; Calcium Signaling ; Phosphates/metabolism
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Contributed Indexing:
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Keywords: Ligand-protein interaction; Myo-D-inositol 1,4,5-trisphosphate; Protein structure; Signal transduction
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Substance Nomenclature:
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0 (Inositol 1,4,5-Trisphosphate Receptors)
0 (Carrier Proteins)
4L6452S749 (Inositol)
0 (Phosphates)
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Entry Date(s):
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Date Created: 20230403 Date Completed: 20230522 Latest Revision: 20230522
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Update Code:
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20240104
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DOI:
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10.1016/j.bbamcr.2023.119470
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PMID:
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37011730
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Conventionally, myo-D-inositol 1, 4,5-trisphosphate (IP 3 ) is thought to exert its second messenger effects through the gating of IP 3 R Ca 2+ release channels, located in Ca 2+ -storage organelles like the endoplasmic reticulum. However, there is considerable indirect evidence to support the concept that IP 3 might interact with other, non-IP 3 R proteins within cells. To explore this possibility further, the Protein Data Bank was searched using the term "IP3". This resulted in the retrieval of 203 protein structures, the majority of which were members of the IP 3 R/ryanodine receptor superfamily of channels. Only 49 of these structures were complexed with IP 3 . These were inspected for their ability to interact with the carbon-1 phosphate of IP 3 , since this is the least accessible phosphate group of its precursor, phosphatidylinositol 4,5-bisphosphate (PI(4,5)P 2 ). This reduced the number of structures retrieved to 35, of which 9 were IP 3 Rs. The remaining 26 structures represent a diverse range of proteins, including inositol-lipid metabolizing enzymes, signal transducers, PH domain containing proteins, cytoskeletal anchor proteins, the TRPV4 ion channel, a retroviral Gag protein and fibroblast growth factor 2. Such proteins may impact on IP 3 signalling and its effects on cell-biology. This represents an area open for exploration in the field of IP 3 signalling.
Competing Interests: Declaration of competing interest I have no conflicts of interest relating to this work.
(Copyright © 2023 The Author(s). Published by Elsevier B.V. All rights reserved.)
