Phospholamban
From Wikipedia, the free encyclopedia
Phospholamban pentamer | ||
Identifiers | ||
---|---|---|
Symbol | Phospholamban | |
Pfam | PF04272 | |
InterPro | IPR005984 | |
SCOP | 1fjk | |
TCDB | 8.A.11 | |
OPM family | 70 | |
OPM protein | 1zll | |
Available PDB structures:
1n7lA:1-52 1plnD:35-52 1k9nA:35-52 1plp :1-24 1zllE:1-52 1kchA:35-52 1pslC:35-52 1fjkA:1-52 1fjpA:1-52 |
Identifiers | |
Symbol | PLN |
Alt. Symbols | PLB |
Entrez | 5350 |
HUGO | 9080 |
OMIM | 172405 |
RefSeq | NM_002667 |
UniProt | P26678 |
Other data | |
Locus | Chr. 6 q22.1 |
Phospholamban is a 52 amino acid integral membrane protein that regulates the Ca2+ pump in cardiac muscle cells.
Dephosphorylated phospholamban interacts with the Sarco/Endoplasmic Reticulum Ca2+ ATPase pump (SERCA) to lower its activity and sensitivity to Ca2+, thus decreasing Ca2+ uptake into the sarcoplasmic reticulum (SR). Phospholamban is phosphorylated by Protein Kinase A, inducing an order-to-disorder transition, activating the SERCA. Thus, when phospholamban is phosphorylated, its interaction with SERCA is reduced, resulting in an increase in Ca2+ transport into the SR.
Because phospholamban is a substrate for PKA, which is activated with beta-adrenergic stimulation, one would expect relaxation to be favored when PKA is activated. However, this also means that more Ca2+ is stored in the SR and thus more is available for release; this would increase contractility.
Gene knockout of phospholamban results in animals with hyperdynamic hearts, with little apparent negative consequence.
[edit] References
- Karim, C. B., T. L. Kirby, Z. Zhang, Y. Nesmelov, and D. D. Thomas. 2004. Phospholamban structural dynamics in lipid bilayers probed by a spin label rigidly coupled to the peptide backbone. Proc Natl Acad Sci USA, 101(40): 14437-14442. Entrez PubMed 15448204
- Brittsan, A. G. & Kranias, E. G. Phospholamban and cardiac contractile function. J. Mol. Cell. Cardiol. 32, 2131-2139 (2000). Entrez PubMed 11112989
[edit] External links
- UMich Orientation of Proteins in Membranes families/superfamily-70 - Orientations of phospholamban and sarcolipin in membrane]
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