Chimaeras reveal the role of the catalytic core in the activation of the plasma membrane Ca2+ pump

Biochemical Journal

Volumn 356, Issue 1, 2001, Pages 241-245

  Ba Thein, William ^a   Caride, Ariel J ^a   Enyedi, Ágnes ^a   Pászty, Katalin ^a   Croy, Cynthia L ^a   Filoteo, Adelaida G ^a   Penniston, John T ^a  

^a MAYO CLINIC   (United States)

Author keywords

Ca2+ signal; Calmodulin; Ion transport; P type ATPase

Indexed keywords

CALCIUM; CATALYSIS; CELL MEMBRANES; ENZYMES; MOLECULES; RATE CONSTANTS;

ISOFORMS;

BIOCHEMISTRY;

CALCIUM ION; CALMODULIN; ISOPROTEIN; MEMBRANE PROTEIN; PLASMA MEMBRANE CALCIUM PUMP PROTEIN; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; AMINO TERMINAL SEQUENCE; ARTICLE; BINDING AFFINITY; CALCIUM TRANSPORT; CARBOXY TERMINAL SEQUENCE; CATALYSIS; CHIMERA; CYTOPLASM; MEMBRANE CHANNEL; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN FUNCTION; PROTEIN STRUCTURE;

CHIMAERA; CHIMAERIFORMES;

EID: 0035874462     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/bj3560241     Document Type: Article

References (12)

1. 2+ pump
2. 2+
3. 2+ pump have different regulatory properties
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5. Crystal structure of the calcium pump of sarcoplasmic reticulum at 2.6 Å resolution
6. 2+ pump isoforms 2 and 3 and prevents binding of calmodulin
7. 2+ pump Isoform 4b by phosphorylation of an inhibitory region downstream of the calmodulin-binding domain
8. 2+ pump is slow and is changed by alternative splicing
9. Biogenesis: Plasma membrane calcium ATPase: 15 years of work on the purified enzyme
10. 2+ pump is controlled by alternative splicing
11. 2+ ATPase. Functional properties of the enzyme and its splicing products
12. 2+ pump isoform 3f is weakly stimulated by calmodulin