Multiple Phosphorylation of Chicken Protein Tyrosine Phosphatase 1 and Human Protein Tyrosine Phosphatase 1B by Casein Kinase II and p60in Vitro
Autor: | Choong Won Kim, Eun Joo Jung, Yoon-Se Kang |
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Rok vydání: | 1998 |
Předmět: |
DNA
Complementary Recombinant Fusion Proteins Molecular Sequence Data Proto-Oncogene Proteins pp60(c-src) Phosphatase Biophysics Gene Expression Protein tyrosine phosphatase In Vitro Techniques Protein Serine-Threonine Kinases Biochemistry Phosphoamino acid analysis Receptor tyrosine kinase Protein Phosphatase 1 Escherichia coli Animals Humans Protein phosphorylation Amino Acid Sequence Cloning Molecular Phosphorylation Casein Kinase II Molecular Biology Binding Sites Base Sequence biology Chemistry Cell Biology Protein phosphatase 2 Molecular biology biology.protein Protein Tyrosine Phosphatases Casein kinase 2 Chickens |
Zdroj: | Biochemical and Biophysical Research Communications. 246:238-242 |
ISSN: | 0006-291X |
DOI: | 10.1006/bbrc.1998.8605 |
Popis: | We have cloned a soluble chicken protein tyrosine phosphatase, named CPTP1, from the cDNA library of chicken intestine. The CPTP1 showed 92% sequence identity to the corresponding 321 amino acid residues of human PTP1B (HPTP1B). CPTP1 lacked 13 amino acids of the N-terminal region compared with HPTP1B, while the C-terminal 48 amino acid sequence of this protein was distinct from those of other PTPs. In vitro phosphorylation and phosphoamino acid analysis showed that both CPTP1 and HPTP1B were phosphorylated on serine and threonine residues near their N-terminus by casein kinase II (CKII). Furthermore, phosphorylation of CPTP1 by CKII resulted in an inhibition of its phosphatase activity in vitro. Interestingly, both CPTP1 and HPTP1B were also tyrosine-phosphorylated near their N-terminus by p60c-src. When we examined the vanadate effect, in the absence of vanadate, the tyrosine-phosphorylated CPTP1 by p60c-src was autodephosphorylated by its own phosphatase activity. These results suggest that both CPTP1 and HPTP1B might play an important role in CKII- and p60c-src-induced signal transduction cascades. |
Databáze: | OpenAIRE |
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