Journal article
Protein tyrosine phosphatase hPTPN20a is targeted to sites of actin polymerization
MT Fodero-Tavoletti, MP Hardy, B Cornell, F Katsis, CM Sadek, CA Mitchell, BE Kemp, T Tiganis
Biochemical Journal | PORTLAND PRESS LTD | Published : 2005
DOI: 10.1042/BJ20041932
Abstract
The human genome encodes 38 classical tyrosine-specific PTPs (protein tyrosine phosphatases). Many PTPs have been shown to regulate fundamental cellular processes and several are mutated in human diseases. We report that the product of the PTPN20 gene at the chromosome locus 10q11.2 is alternatively spliced to generate 16 possible variants of the classical human non-transmembrane PTP 20 (hPTPN20). One of these variants, hPTPN20a, was expressed in a wide range of both normal and transformed cell lines. The catalytic domain of hPTPN20 exhibited catalytic activity towards tyrosyl phosphorylated substrates, confirming that it is a bona fide PTP. In serum-starved COS1 cells, hPTPN20a was targeted..
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