Title : Inhibition of protein-tyrosine phosphatase stimulates the dynamin-dependent endocytosis of ROMK1.

Pub. Date : 2002 Feb 8

PMID : 11719519






6 Functional Relationships(s)
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1 We have now used confocal microscopy, the patch clamp technique, and biotin labeling to further examine the role of tyrosine phosphorylation in regulating ROMK1 trafficking. Tyrosine potassium inwardly rectifying channel subfamily J member 1 Homo sapiens
2 The notion that the effect of PAO is mediated by stimulating tyrosine phosphorylation-induced endocytosis of ROMK1 has also been supported by findings that mutating the tyrosine residue 337 of ROMK1 to alanine abolished the effect of PAO. Tyrosine potassium inwardly rectifying channel subfamily J member 1 Homo sapiens
3 The notion that the effect of PAO is mediated by stimulating tyrosine phosphorylation-induced endocytosis of ROMK1 has also been supported by findings that mutating the tyrosine residue 337 of ROMK1 to alanine abolished the effect of PAO. Tyrosine potassium inwardly rectifying channel subfamily J member 1 Homo sapiens
4 The notion that the effect of PAO is mediated by stimulating tyrosine phosphorylation-induced endocytosis of ROMK1 has also been supported by findings that mutating the tyrosine residue 337 of ROMK1 to alanine abolished the effect of PAO. Tyrosine potassium inwardly rectifying channel subfamily J member 1 Homo sapiens
5 The notion that the effect of PAO is mediated by stimulating tyrosine phosphorylation-induced endocytosis of ROMK1 has also been supported by findings that mutating the tyrosine residue 337 of ROMK1 to alanine abolished the effect of PAO. Tyrosine potassium inwardly rectifying channel subfamily J member 1 Homo sapiens
6 This indicates that the tyrosine phosphorylation-induced endocytosis of ROMK1 is dynamin-dependent. Tyrosine potassium inwardly rectifying channel subfamily J member 1 Homo sapiens