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PMID: 8988251 Published · ppublish English Journal Article Review

The plasma membrane calcium pump: recent developments and future perspectives.

Experientia ·Vol. 52 ·No. 12 ·1996-12-15 ·Pages 1091-100

Carafoli E, Garcia-Martin E, Guerini D

Abstract

The Ca2+ pump of the plasma membrane (PMCA) is regulated by a number of agents. The most important is calmodulin (CaM), which binds to a domain located in the C-terminal portion of the pump, removing it from an autoinhibitory site next to the active site. The CaM-binding domain is preceded by an acidic sequence which contains a hidden signal for endoplasmic reticulum (ER) retention. Chimeras of the PMCA and endoplasmic reticulum (SERCA) pumps have revealed the presence of a strong signal for ER retention in the first 45 residues of the SERCA pump. Four gene products of the PMCA pump are known: two of them (1 and 4) are ubiquitously expressed, two (2 and 3) are specific for nerve cells and may be induced by their activation. Mutagenesis work has identified four residues in three of the transmembrane domains of the pump which may be components of the trans-protein Ca2+ path. The mutation of two of these residues alters the membrane targeting of the pump.

MeSH Terms
Amino Acid Sequence Calcium/metabolism Calcium-Transporting ATPases/chemistry,metabolism Calpain/metabolism Cell Membrane/chemistry Conserved Sequence/genetics Immunohistochemistry Models, Molecular Molecular Sequence Data Protein Structure, Secondary Recombinant Fusion Proteins/chemistry
Chemicals
Recombinant Fusion Proteins Calpain Calcium-Transporting ATPases Calcium
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Carafoli E
Inst. for Biochemistry III, ETH Zurich, Switzerland.
Garcia-Martin E
Guerini D
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Article Info
Journal
Experientia
Abbr.
Experientia
ISSN
0014-4754
DOI
10.1007/BF01952107
Published
1996-12-15
Pages
1091-100
Language
English
Region
Switzerland
NLM ID
0376547
Subset
IM
External Links
PubMed source DOI: 10.1007/BF01952107
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