PKC modulation of minK current involves multiple phosphorylation sites

Annals of the New York Academy of Sciences

Volumn 868, Issue , 1999, Pages 431-433

  Lo, C Frederick ^a   Numann, Randy ^a  

^a PFIZER INC   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

COMPLEMENTARY DNA; POTASSIUM ION; PROTEIN KINASE C;

ACTION POTENTIAL; ANIMAL CELL; CONFERENCE PAPER; CONTROLLED STUDY; MUTAGENESIS; NONHUMAN; OOCYTE; POTASSIUM CURRENT; PROTEIN PHOSPHORYLATION;

ANIMALIA; MUSTELA VISON;

EID: 0033007571     PISSN: 00778923     EISSN: None     Source Type: Book Series    
DOI: 10.1111/j.1749-6632.1999.tb11307.x     Document Type: Conference Paper

References (5)

1. Sanguinetti, M.C. et al. 1996. Coassembly of KvLQT1 and minK (IsK.) proteins to form cardiac Iks potassium channel. Nature 384: 80-83.
2. Splawski, I. et al. 1997. Mutations in the hminK gene cause long QT syndrome and suppress Iks function. Nat. Genet. 17: 338-340.
3. + channel in mouse heart. EMBO J. 10: 2805-2811.
4. Varnum, M.D. et al. 1993. The minK channel underlies the cardiac potassium current Iks and mediates species-specific responses to protein kinase C. Proc. Natl. Acad. Sci. USA 90: 11528-11532.
5. + currents expressed from the guinea pig cardiac IsK protein are enhanced by activators of proteinkinase C. Proc. Natl. Acad. Sci. USA 91: 1766-1770.