SH3GLB1

File:Endophilin-b1-helical-scaffold.png{{cite journal | vauthors = Pettersen EF, Goddard TD, Huang CC, Meng EC, Couch GS, Croll TI, Morris JH, Ferrin TE | display-authors = 6 | title = UCSF ChimeraX: Structure visualization for researchers, educators, and developers | journal = Protein Science | volume = 30 | issue = 1 | pages = 70–82 | date = January 2021 | pmid = 32881101 | pmc = 7737788 | doi = 10.1002/pro.3943 }} rendering of [https://www.ebi.ac.uk/pdbe/entry/pdb/6up6 6UP6].]]

In the presence of model biological membranes, endophilin-B1 dimers assemble into helical scaffolds around the membrane and drive its tubulation.

In addition to the membrane binding and remodeling properties endophilin-B1 shares with many other BAR proteins, endophilin-B1 interacts with the pro-apoptotic factor Bcl-2-associated X protein (Bax) and SH3GLB2. It has also been shown to interact with a wide variety of proteins through a canonical SH3 domain that enables PxxP motif-containing protein interactions, including Beclin-1, amphiphysin-1, amphiphysin-2, and huntingtin.{{cite journal | vauthors = Toton E, Lisiak N, Sawicka P, Rybczynska M | title = Beclin-1 and its role as a target for anticancer therapy | journal = Journal of Physiology and Pharmacology | volume = 65 | issue = 4 | pages = 459–467 | date = August 2014 | pmid = 25179078 | url = https://pubmed.ncbi.nlm.nih.gov/25179078 }}{{cite journal | vauthors = Modregger J, Schmidt AA, Ritter B, Huttner WB, Plomann M | title = Characterization of Endophilin B1b, a brain-specific membrane-associated lysophosphatidic acid acyl transferase with properties distinct from endophilin A1 | journal = The Journal of Biological Chemistry | volume = 278 | issue = 6 | pages = 4160–4167 | date = February 2003 | pmid = 12456676 | doi = 10.1074/jbc.M208568200 | doi-access = free }}

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