L-Lactate Dehydrogenase Identified as a Protein Tyrosine Phosphatase 1B Substrate by Using K-BIPS.
Ontology highlight
ABSTRACT: Kinases and phosphatases are major players in a variety of cellular events, including cell signaling. Aberrant activity or mutations in kinases and phosphatases can lead to diseases such as cancer, diabetes, and Alzheimer's. Compared to kinases, phosphatases are understudied; this is partly a result of the limited methods for identifying substrates. As a solution, we developed a proteomics-based method called kinase-catalyzed biotinylation to identify phosphatase substrates (K-BIPS) that previously identified substrates of Ser/Thr phosphatases using small molecule inhibitors. Here, for the first time, K-BIPS was applied to identify substrates of a tyrosine phosphatase, protein tyrosine phosphatase 1B (PTP1B), under siRNA knockdown conditions. Eight possible substrates of PTP1B were discove
SUBMITTER: Acharige NPN
PROVIDER: S-EPMC8104301 | biostudies-literature | 2021 Jan
REPOSITORIES: biostudies-literature
ACCESS DATA