Cell and molecular biology of the novel protein tyrosine-phosphatase-interacting protein 51.
This chapter examines the current state of knowledge about the expression profile, as well as biochemical properties and biological functions of the evolutionarily conserved protein PTPIP51. PTPIP51 is apparently expressed in splice variants and shows a particularly high expression in epithelia, skeletal muscle, placenta, and germ cells, as well as during mammalian development and in cancer. PTPIP51 is an in vitro substrate of Src- and protein kinase A, the PTP1B/TCPTP protein tyrosine phosphatases and interacts with 14-3-3 proteins, the Nuf2 kinetochore protein, the ninein-interacting CGI-99 protein, diacylglycerol kinase alpha, and also with itself forming dimers and trimers. Although the precise cellular function remains to be elucidated, the current data implicate PTPIP51 in signaling cascades mediating proliferation, differentiation, apoptosis, and motility.
Stenzinger
Albrecht
A
Institute of Anatomy and Cell Biology, Justus-Liebig-University, Giessen, Germany.
Schreiner
Dietmar
D
Koch
Philipp
P
Hofer
Hans-Werner
HW
Wimmer
Monika
M
D000595:Amino Acid Sequence; D022082:Cellular Structures; D006801:Humans; D024101:Mitochondrial Proteins / Q000502:physiology*; D008967:Molecular Biology; D008969:Molecular Sequence Data; D017027:Protein Tyrosine Phosphatases / Q000502:physiology*; D017386:Sequence Homology, Amino Acid; D015398:Signal Transduction
D024101:Mitochondrial Proteins; D017027:Protein Tyrosine Phosphatases; C515449:RMDN3 protein, human