Shape shifting: The multiple conformational substates of the PTEN N-terminal PIP₂ -binding domain.

ABSTRACT: The Phosphatase and TENsin homolog deleted on chromosome 10 (PTEN) is a chief regulator of a variety of cellular processes including cell proliferation, migration, growth, and death. It is also a major tumor suppressor gene that is frequently mutated or lost under cancerous conditions. PTEN encodes a dual-specificity (lipid and protein) phosphatase that negatively regulates the PI3K/AKT/mTOR signaling pathway where the PIP₂ -binding domain (PBD) regulates the lipid phosphatase function. Unfortunately, despite two decades of research, a full-length structure of PTEN remains elusive, leaving open questions regarding PTEN's disordered regions that mediate protein stability, post-translational modifications, protein-protein interactions, while also hindering the design of small mole

SUBMITTER: Dawson JE 

PROVIDER: S-EPMC9004235 | biostudies-literature | 2022 May

REPOSITORIES: biostudies-literature