期刊
NEURON
卷 96, 期 4, 页码 827-+出版社
CELL PRESS
DOI: 10.1016/j.neuron.2017.09.038
关键词
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资金
- DFG [SFB 746, TP 16, Fa 332/9-1, TRR152, TP 20, BIOSS-2]
- Swiss National Science Foundation [CRSII3_154411 / I]
- National Institutes for Health [U42OD011174, U54HG006348]
- Swiss National Science Foundation (SNF) [CRSII3_154411] Funding Source: Swiss National Science Foundation (SNF)
Plasma membrane Ca2+-ATPases (PMCAs), a family of P-type ATPases, extrude Ca2+ ions from the cytosol to the extracellular space and are considered to be key regulators of Ca2+ signaling. Here we show by functional proteomics that native PMCAs are heteromeric complexes that are assembled from two pore-forming PMCA1-4 subunits and two of the single-span membrane proteins, either neuroplastin or basigin. Contribution of the two Ig domain-containing proteins varies among different types of cells and along postnatal development. Complex formation of neuroplastin or basigin with PMCAs1-4 occurs in the endoplasmic reticulum and is obligatory for stability of the PMCA proteins and for delivery of PMCA complexes to the surface membrane. Knockout and (over)-expression of both neuroplastin and basigin profoundly affect the time course of PMCA-mediated Ca2+ transport, as well as submembraneous Ca2+ concentrations under steady-state conditions. Together, these results establish neuroplastin and basigin as obligatory auxiliary subunits of native PMCAs and key regulators of intracellular Ca2+ concentration.
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