Structure of the human plasma membrane Ca2+-ATPase 1 in complex with its obligatory subunit neuroplastin.

Abstract:

:Plasma membrane Ca2+-ATPases (PMCAs) are key regulators of global Ca2+ homeostasis and local intracellular Ca2+ dynamics. Recently, Neuroplastin (NPTN) and basigin were identified as previously unrecognized obligatory subunits of PMCAs that dramatically increase the efficiency of PMCA-mediated Ca2+ clearance. Here, we report the cryo-EM structure of human PMCA1 (hPMCA1) in complex with NPTN at a resolution of 4.1 Å for the overall structure and 3.9 Å for the transmembrane domain. The single transmembrane helix of NPTN interacts with the TM8-9-linker and TM10 of hPMCA1. The subunits are required for the hPMCA1 functional activity. The NPTN-bound hPMCA1 closely resembles the E1-Mg2+ structure of endo(sarco)plasmic reticulum Ca2+ ATPase and the Ca2+ site is exposed through a large open cytoplasmic pathway. This structure provides insight into how the subunits bind to the PMCAs and serves as an important basis for understanding the functional mechanisms of this essential calcium pump family.

journal_name

Nat Commun

journal_title

Nature communications

authors

Gong D,Chi X,Ren K,Huang G,Zhou G,Yan N,Lei J,Zhou Q

doi

10.1038/s41467-018-06075-7

subject

Has Abstract

pub_date

2018-09-06 00:00:00

pages

3623

issue

1

issn

2041-1723

pii

10.1038/s41467-018-06075-7

journal_volume

9

pub_type

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