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STIM-TRP Pathways and Microdomain Organization: Contribution of TRPC1 in Store-Operated Ca2+ Entry: Impact on Ca2+ Signaling and Cell Function.
Adv Exp Med Biol. 2017; 993:159-188.AE

Abstract

Store-operated calcium entry (SOCE) is a ubiquitous Ca2+ entry pathway that is activated in response to depletion of ER-Ca2+ stores and critically controls the regulation of physiological functions in a wide variety of cell types. The transient receptor potential canonical (TRPC) channels (TRPCs 1-7), which are activated by stimuli leading to PIP2 hydrolysis, were first identified as molecular components of SOCE channels. While TRPC1 was associated with SOCE and regulation of function in several cell types, none of the TRPC members displayed I CRAC, the store-operated current identified in lymphocytes and mast cells. Intensive search finally led to the identification of Orai1 and STIM1 as the primary components of the CRAC channel. Orai1 was established as the pore-forming channel protein and STIM1 as the ER-Ca2+ sensor protein involved in activation of Orai1. STIM1 also activates TRPC1 via a distinct domain in its C-terminus. However, TRPC1 function depends on Orai1-mediated Ca2+ entry, which triggers recruitment of TRPC1 into the plasma membrane where it is activated by STIM1. TRPC1 and Orai1 form distinct store-operated Ca2+ channels that regulate specific cellular functions. It is now clearly established that regulation of TRPC1 trafficking can change plasma membrane levels of the channel, the phenotype of the store-operated Ca2+ current, as well as pattern of SOCE-mediated [Ca2+]i signals. Thus, TRPC1 is activated downstream of Orai1 and modifies the initial [Ca2+]i signal generated by Orai1. This review will highlight current concepts of the activation and regulation of TRPC1 channels and its impact on cell function.

Authors+Show Affiliations

Secretory Physiology Section, Molecular Physiology and Therapeutics Branch, National Institute of Dental and Craniofacial Research - NIDCR, National Institutes of Health - NIH, Building 10, Room 1N-113, Bethesda, MD, 20892, USA. ongh@mail.nih.gov.Secretory Physiology Section, Molecular Physiology and Therapeutics Branch, National Institute of Dental and Craniofacial Research - NIDCR, National Institutes of Health - NIH, Building 10, Room 1N-113, Bethesda, MD, 20892, USA. indu.ambudkar@nih.gov.

Pub Type(s)

Journal Article
Research Support, N.I.H., Intramural
Review

Language

eng

PubMed ID

28900914

Citation

Ong, Hwei Ling, and Indu S. Ambudkar. "STIM-TRP Pathways and Microdomain Organization: Contribution of TRPC1 in Store-Operated Ca2+ Entry: Impact On Ca2+ Signaling and Cell Function." Advances in Experimental Medicine and Biology, vol. 993, 2017, pp. 159-188.
Ong HL, Ambudkar IS. STIM-TRP Pathways and Microdomain Organization: Contribution of TRPC1 in Store-Operated Ca2+ Entry: Impact on Ca2+ Signaling and Cell Function. Adv Exp Med Biol. 2017;993:159-188.
Ong, H. L., & Ambudkar, I. S. (2017). STIM-TRP Pathways and Microdomain Organization: Contribution of TRPC1 in Store-Operated Ca2+ Entry: Impact on Ca2+ Signaling and Cell Function. Advances in Experimental Medicine and Biology, 993, 159-188. https://doi.org/10.1007/978-3-319-57732-6_9
Ong HL, Ambudkar IS. STIM-TRP Pathways and Microdomain Organization: Contribution of TRPC1 in Store-Operated Ca2+ Entry: Impact On Ca2+ Signaling and Cell Function. Adv Exp Med Biol. 2017;993:159-188. PubMed PMID: 28900914.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - STIM-TRP Pathways and Microdomain Organization: Contribution of TRPC1 in Store-Operated Ca2+ Entry: Impact on Ca2+ Signaling and Cell Function. AU - Ong,Hwei Ling, AU - Ambudkar,Indu S, PY - 2017/9/14/entrez PY - 2017/9/14/pubmed PY - 2017/12/6/medline KW - Caveolin KW - ER-PM junctions KW - Lipid rafts KW - Orai1 KW - SOCE KW - STIM1 KW - TRPC SP - 159 EP - 188 JF - Advances in experimental medicine and biology JO - Adv. Exp. Med. Biol. VL - 993 N2 - Store-operated calcium entry (SOCE) is a ubiquitous Ca2+ entry pathway that is activated in response to depletion of ER-Ca2+ stores and critically controls the regulation of physiological functions in a wide variety of cell types. The transient receptor potential canonical (TRPC) channels (TRPCs 1-7), which are activated by stimuli leading to PIP2 hydrolysis, were first identified as molecular components of SOCE channels. While TRPC1 was associated with SOCE and regulation of function in several cell types, none of the TRPC members displayed I CRAC, the store-operated current identified in lymphocytes and mast cells. Intensive search finally led to the identification of Orai1 and STIM1 as the primary components of the CRAC channel. Orai1 was established as the pore-forming channel protein and STIM1 as the ER-Ca2+ sensor protein involved in activation of Orai1. STIM1 also activates TRPC1 via a distinct domain in its C-terminus. However, TRPC1 function depends on Orai1-mediated Ca2+ entry, which triggers recruitment of TRPC1 into the plasma membrane where it is activated by STIM1. TRPC1 and Orai1 form distinct store-operated Ca2+ channels that regulate specific cellular functions. It is now clearly established that regulation of TRPC1 trafficking can change plasma membrane levels of the channel, the phenotype of the store-operated Ca2+ current, as well as pattern of SOCE-mediated [Ca2+]i signals. Thus, TRPC1 is activated downstream of Orai1 and modifies the initial [Ca2+]i signal generated by Orai1. This review will highlight current concepts of the activation and regulation of TRPC1 channels and its impact on cell function. SN - 0065-2598 UR - https://www.unboundmedicine.com/medline/citation/28900914/STIM_TRP_Pathways_and_Microdomain_Organization:_Contribution_of_TRPC1_in_Store_Operated_Ca2+_Entry:_Impact_on_Ca2+_Signaling_and_Cell_Function_ L2 - https://dx.doi.org/10.1007/978-3-319-57732-6_9 DB - PRIME DP - Unbound Medicine ER -