Endophilin-B1 is a protein that in humans is encoded by the SH3GLB1 gene. Endophilin-B1 belongs to the Bin/Amphiphysin/Rvs167 (BAR) family of proteins and plays a critical role in mitochondrial fission and fusion, as well as in autophagy and apoptosis. Loss of functional endophilin-B1 is seen in many different forms of cancer. The link between carcinogenesis and dysregulation of cell death pathways suggests that endophilin-B1 serves a critical tumor suppressor role in the cell, although the underlying mechanisms are not known.
This gene encodes a SRC homology 3 domain-containing protein. The encoded protein interacts with the proapoptotic member of the Bcl-2 family, Bcl-2-associated X protein (Bax) and may be involved in regulating apoptotic signaling pathways. This protein may also be involved in maintaining mitochondrial morphology. Alternate splicing results in multiple transcript variants. [provided by RefSeq, Sep 2011].
via MyGene.info
Endophilin-B1 is a protein that in humans is encoded by the SH3GLB1 gene. Endophilin-B1 belongs to the Bin/Amphiphysin/Rvs167 (BAR) family of proteins and plays a critical role in mitochondrial fission and fusion, as well as in autophagy and apoptosis. Loss of functional endophilin-B1 is seen in many different forms of cancer. The link between carcinogenesis and dysregulation of cell death pathways suggests that endophilin-B1 serves a critical tumor suppressor role in the cell, although the underlying mechanisms are not known.
== Structure == thumb|left|A pseudo-atomic model of helical scaffolds formed by a truncated form of endophilin-B1. Based on a [[UCSF Chimera|ChimeraX rendering of 6UP6.]] In the presence of model biological membranes, endophilin-B1 dimers assemble into helical scaffolds around the membrane and drive its tubulation.
Discovered by embedding cosine similarity (sentence-transformers MiniLM, 384-dim).