دورية أكاديمية
أعرض في EDS

CNNM proteins selectively bind to the TRPM7 channel to stimulate divalent cation entry into cells.

التفاصيل البيبلوغرافية
العنوان: CNNM proteins selectively bind to the TRPM7 channel to stimulate divalent cation entry into cells.
المؤلفون: Bai Z; Rutgers-Robert Wood Johnson Medical School, Piscataway, New Jersey, United States of America., Feng J; UCONN Health Center, Farmington, New Mexico, United States of America., Franken GAC; Radboud University Medical Center, Nijmegen, the Netherlands., Al'Saadi N; Rutgers-Robert Wood Johnson Medical School, Piscataway, New Jersey, United States of America.; University of Misan, Amarah, Iraq., Cai N; Rutgers-Robert Wood Johnson Medical School, Piscataway, New Jersey, United States of America., Yu AS; UCONN Health Center, Farmington, New Mexico, United States of America., Lou L; Rutgers-Robert Wood Johnson Medical School, Piscataway, New Jersey, United States of America., Komiya Y; Rutgers-Robert Wood Johnson Medical School, Piscataway, New Jersey, United States of America., Hoenderop JGJ; Radboud University Medical Center, Nijmegen, the Netherlands., de Baaij JHF; Radboud University Medical Center, Nijmegen, the Netherlands., Yue L; UCONN Health Center, Farmington, New Mexico, United States of America., Runnels LW; Rutgers-Robert Wood Johnson Medical School, Piscataway, New Jersey, United States of America.
المصدر: PLoS biology [PLoS Biol] 2021 Dec 20; Vol. 19 (12), pp. e3001496. Date of Electronic Publication: 2021 Dec 20 (Print Publication: 2021).
نوع المنشور: Journal Article; Research Support, N.I.H., Extramural
اللغة: English
بيانات الدورية: Publisher: Public Library of Science Country of Publication: United States NLM ID: 101183755 Publication Model: eCollection Cited Medium: Internet ISSN: 1545-7885 (Electronic) Linking ISSN: 15449173 NLM ISO Abbreviation: PLoS Biol Subsets: MEDLINE
أسماء مطبوعة: Original Publication: San Francisco, CA : Public Library of Science, [2003]-
مواضيع طبية MeSH: Cation Transport Proteins/*metabolism , Cyclins/*metabolism , Protein Serine-Threonine Kinases/*metabolism , TRPM Cation Channels/*metabolism, Cation Transport Proteins/physiology ; Cations, Divalent/metabolism ; Cell Line, Tumor ; Cyclins/physiology ; HEK293 Cells ; Humans ; Magnesium/metabolism ; Patch-Clamp Techniques ; Protein Serine-Threonine Kinases/physiology ; TRPM Cation Channels/genetics ; TRPM Cation Channels/physiology
مستخلص: Magnesium is essential for cellular life, but how it is homeostatically controlled still remains poorly understood. Here, we report that members of CNNM family, which have been controversially implicated in both cellular Mg2+ influx and efflux, selectively bind to the TRPM7 channel to stimulate divalent cation entry into cells. Coexpression of CNNMs with the channel markedly increased uptake of divalent cations, which is prevented by an inactivating mutation to the channel's pore. Knockout (KO) of TRPM7 in cells or application of the TRPM7 channel inhibitor NS8593 also interfered with CNNM-stimulated divalent cation uptake. Conversely, KO of CNNM3 and CNNM4 in HEK-293 cells significantly reduced TRPM7-mediated divalent cation entry, without affecting TRPM7 protein expression or its cell surface levels. Furthermore, we found that cellular overexpression of phosphatases of regenerating liver (PRLs), known CNNMs binding partners, stimulated TRPM7-dependent divalent cation entry and that CNNMs were required for this activity. Whole-cell electrophysiological recordings demonstrated that deletion of CNNM3 and CNNM4 from HEK-293 cells interfered with heterologously expressed and native TRPM7 channel function. We conclude that CNNMs employ the TRPM7 channel to mediate divalent cation influx and that CNNMs also possess separate TRPM7-independent Mg2+ efflux activities that contribute to CNNMs' control of cellular Mg2+ homeostasis.
Competing Interests: The authors have declared that no competing interests exist.
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معلومات مُعتمدة: R01 HL147350 United States HL NHLBI NIH HHS
المشرفين على المادة: 0 (CNNM3 protein, human)
0 (CNNM4 protein, human)
0 (Cation Transport Proteins)
0 (Cations, Divalent)
0 (Cyclins)
0 (TRPM Cation Channels)
EC 2.7.11.1 (Protein Serine-Threonine Kinases)
EC 2.7.11.1 (TRPM7 protein, human)
I38ZP9992A (Magnesium)
تواريخ الأحداث: Date Created: 20211220 Date Completed: 20220211 Latest Revision: 20220211
رمز التحديث: 20231215
مُعرف محوري في PubMed: PMC8726484
DOI: 10.1371/journal.pbio.3001496
PMID: 34928937
قاعدة البيانات: MEDLINE
الوصف
تدمد:1545-7885
DOI:10.1371/journal.pbio.3001496