Abstract：
:In HEK293 cells, transfected with the Ca2+ channel protein TRPV6, Ca2+ influx is increased and TRPV6 is tyrosine phosphorylated following addition of the tyrosine phosphatase inhibitor N,N-dimethyl-hydroxamido hydroxovanadate to cells. This effect of DMHV is enhanced by co-transfection of cells with the tyrosine kinase Src and the tyrosine phosphatase 1B. It is abolished when cells had been treated with PP1, an inhibitor of Src family tyrosine kinases. PTP1B interacts with the N-terminal domain of TRPV6 within a region of amino acids 1-191 as shown by co-immunoprecipitation, bimolecular fluorescence complementation and the yeast 2-hybrid system. Point mutation of both tyrosines 161 and 162 in the TRPV6 protein abolishes the DMHV-effect on Ca2+ influx and tyrosine phosphorylation by Src. Single mutations of Y161 or Y162 shows that each of both tyrosines alone is sufficient for the DMHV-effect. We conclude that phosphorylation/dephosphorylation of tyrosines in position 161 and 162 is essential for regulation of Ca2+ influx through TRPV6 Ca2+ channels in HEK293 cells.
journal_name
Cell Calciumjournal_title
Cell calciumauthors
Sternfeld L,Anderie I,Schmid A,Al-Shaldi H,Krause E,Magg T,Schreiner D,Hofer HW,Schulz Idoi
10.1016/j.ceca.2006.11.008subject
Has Abstractpub_date
2007-07-01 00:00:00pages
91-102issue
1eissn
0143-4160issn
1532-1991pii
S0143-4160(06)00218-1journal_volume
42pub_type
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