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SH3 domain containing GRB2 like, endophilin B1 (SH3GLB1, also known as Endophilin-B1 or Bif-1) is a membrane remodeling protein crucial for mitochondrial fission/fusion, autophagy, and apoptosis. It contains both an N-BAR domain (for membrane curvature and dimerization) and a C-terminal SH3 domain (enabling interactions with proteins bearing proline-rich regions). SH3GLB1 promotes the formation of autophagosomes through modulation of PI3KC3 and interacts with apoptosis regulators such as Bax. Dysregulation of SH3GLB1 is linked to cancer (as a putative tumor suppressor) and impacts cell death pathways in both neuronal and non-neuronal cells[1][3][5].
Not directly established. By analogy: - Modulation of Bax/Bcl-2 interactions - Regulation of PI3KC3 (class III phosphatidylinositol 3-kinase) activity - Influence on autophagy induction - Drugs targeting upstream or downstream effectors in these pathways may indirectly affect SH3GLB1 activity.
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