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Hold the door: hPMCA1/neuroplastin interactions regulate Ca2+-binding site accessibility.


ABSTRACT: In a September 2018 paper published in Nature Communications, Gong et al. identified the domains through which human PMCA1 and neuroplastin (NPTN) interact. Upon binding, hPMCA1 TM domains separate T110 in TM1 and A370 in TM3 to reveal the Ca2+-binding site. Thus, NPTN is able to directly modulate the accessibility of cytosolic Ca2+ to PMCA.

SUBMITTER: Go CK 

PROVIDER: S-EPMC6309627 | biostudies-literature | 2018 Dec

REPOSITORIES: biostudies-literature

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Hold the door: hPMCA1/neuroplastin interactions regulate Ca<sup>2+</sup>-binding site accessibility.

Go Christina K CK   Soboloff Jonathan J  

Cell calcium 20181101


In a September 2018 paper published in Nature Communications, Gong et al. identified the domains through which human PMCA1 and neuroplastin (NPTN) interact. Upon binding, hPMCA1 TM domains separate T110 in TM1 and A370 in TM3 to reveal the Ca<sup>2+</sup>-binding site. Thus, NPTN is able to directly modulate the accessibility of cytosolic Ca<sup>2+</sup> to PMCA. ...[more]

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