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STIM Proteins and Regulation of SOCE in ER-PM Junctions

ER-PM junctions are membrane contact sites formed by the endoplasmic reticulum (ER) and plasma membrane (PM) in close apposition together. The formation and stability of these junctions are dependent on constitutive and dynamic enrichment of proteins, which either contribute to junctional stability...

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Detalles Bibliográficos
Autores principales: Ahmad, Moaz, Narayanasamy, Sasirekha, Ong, Hwei Ling, Ambudkar, Indu
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9405863/
https://www.ncbi.nlm.nih.gov/pubmed/36009047
http://dx.doi.org/10.3390/biom12081152
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author Ahmad, Moaz
Narayanasamy, Sasirekha
Ong, Hwei Ling
Ambudkar, Indu
author_facet Ahmad, Moaz
Narayanasamy, Sasirekha
Ong, Hwei Ling
Ambudkar, Indu
author_sort Ahmad, Moaz
collection PubMed
description ER-PM junctions are membrane contact sites formed by the endoplasmic reticulum (ER) and plasma membrane (PM) in close apposition together. The formation and stability of these junctions are dependent on constitutive and dynamic enrichment of proteins, which either contribute to junctional stability or modulate the lipid levels of both ER and plasma membranes. The ER-PM junctions have come under much scrutiny recently as they serve as hubs for assembling the Ca(2+) signaling complexes. This review summarizes: (1) key findings that underlie the abilities of STIM proteins to accumulate in ER-PM junctions; (2) the modulation of Orai/STIM complexes by other components found within the same junction; and (3) how Orai1 channel activation is coordinated and coupled with downstream signaling pathways.
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spelling pubmed-94058632022-08-26 STIM Proteins and Regulation of SOCE in ER-PM Junctions Ahmad, Moaz Narayanasamy, Sasirekha Ong, Hwei Ling Ambudkar, Indu Biomolecules Review ER-PM junctions are membrane contact sites formed by the endoplasmic reticulum (ER) and plasma membrane (PM) in close apposition together. The formation and stability of these junctions are dependent on constitutive and dynamic enrichment of proteins, which either contribute to junctional stability or modulate the lipid levels of both ER and plasma membranes. The ER-PM junctions have come under much scrutiny recently as they serve as hubs for assembling the Ca(2+) signaling complexes. This review summarizes: (1) key findings that underlie the abilities of STIM proteins to accumulate in ER-PM junctions; (2) the modulation of Orai/STIM complexes by other components found within the same junction; and (3) how Orai1 channel activation is coordinated and coupled with downstream signaling pathways. MDPI 2022-08-20 /pmc/articles/PMC9405863/ /pubmed/36009047 http://dx.doi.org/10.3390/biom12081152 Text en © 2022 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/).
spellingShingle Review
Ahmad, Moaz
Narayanasamy, Sasirekha
Ong, Hwei Ling
Ambudkar, Indu
STIM Proteins and Regulation of SOCE in ER-PM Junctions
title STIM Proteins and Regulation of SOCE in ER-PM Junctions
title_full STIM Proteins and Regulation of SOCE in ER-PM Junctions
title_fullStr STIM Proteins and Regulation of SOCE in ER-PM Junctions
title_full_unstemmed STIM Proteins and Regulation of SOCE in ER-PM Junctions
title_short STIM Proteins and Regulation of SOCE in ER-PM Junctions
title_sort stim proteins and regulation of soce in er-pm junctions
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9405863/
https://www.ncbi.nlm.nih.gov/pubmed/36009047
http://dx.doi.org/10.3390/biom12081152
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