Endophilin-B1 is a protein that in humans is encoded by the SH3GLB1gene.[5][6][7] 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.[8][9][10] Loss of functional endophilin-B1 is seen in many different forms of cancer.[11][12][13] 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
A pseudo-atomic model of helical scaffolds formed by a truncated form of endophilin-B1.[14] Based on a ChimeraX[15] rendering of 6UP6.
In the presence of model biological membranes, endophilin-B1 dimers assemble into helical scaffolds around the membrane and drive its tubulation.[14]
Interactions
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)[5][6] and SH3GLB2.[5] 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.[16][17]
References
^ abcGRCh38: Ensembl release 89: ENSG00000097033 – Ensembl, May 2017
^ abcGRCm38: Ensembl release 89: ENSMUSG00000037062 – Ensembl, May 2017
^"Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^"Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ abcPierrat B, Simonen M, Cueto M, Mestan J, Ferrigno P, Heim J (January 2001). "SH3GLB, a new endophilin-related protein family featuring an SH3 domain". Genomics. 71 (2): 222–234. doi:10.1006/geno.2000.6378. PMID 11161816.
^ abCuddeback SM, Yamaguchi H, Komatsu K, Miyashita T, Yamada M, Wu C, et al. (June 2001). "Molecular cloning and characterization of Bif-1. A novel Src homology 3 domain-containing protein that associates with Bax". The Journal of Biological Chemistry. 276 (23): 20559–20565. doi:10.1074/jbc.M101527200. PMID 11259440.
^Takahashi Y, Coppola D, Matsushita N, Cualing HD, Sun M, Sato Y, et al. (October 2007). "Bif-1 interacts with Beclin 1 through UVRAG and regulates autophagy and tumorigenesis". Nature Cell Biology. 9 (10): 1142–1151. doi:10.1038/ncb1634. PMC 2254521. PMID 17891140.
^Karbowski M, Jeong SY, Youle RJ (September 2004). "Endophilin B1 is required for the maintenance of mitochondrial morphology". The Journal of Cell Biology. 166 (7): 1027–1039. doi:10.1083/jcb.200407046. PMC 2172012. PMID 15452144.
^Takahashi Y, Karbowski M, Yamaguchi H, Kazi A, Wu J, Sebti SM, et al. (November 2005). "Loss of Bif-1 suppresses Bax/Bak conformational change and mitochondrial apoptosis". Molecular and Cellular Biology. 25 (21): 9369–9382. doi:10.1128/MCB.25.21.9369-9382.2005. PMC 1265816. PMID 16227588.
^Coppola D, Khalil F, Eschrich SA, Boulware D, Yeatman T, Wang HG (November 2008). "Down-regulation of Bax-interacting factor-1 in colorectal adenocarcinoma". Cancer. 113 (10): 2665–2670. doi:10.1002/cncr.23892. PMC 2614910. PMID 18833585.
^Coppola D, Helm J, Ghayouri M, Malafa MP, Wang HG (April 2011). "Down-regulation of Bax-interacting factor 1 in human pancreatic ductal adenocarcinoma". Pancreas. 40 (3): 433–437. doi:10.1097/MPA.0b013e318205eb03. PMC 3063470. PMID 21283040.
^ abBhatt VS, Ashley R, Sundborger-Lunna A (January 2021). "Amphipathic Motifs Regulate N-BAR Protein Endophilin B1 Auto-inhibition and Drive Membrane Remodeling". Structure. 29 (1): 61–69.e3. doi:10.1016/j.str.2020.09.012. PMID 33086035. S2CID 224821920.
^Pettersen EF, Goddard TD, Huang CC, Meng EC, Couch GS, Croll TI, et al. (January 2021). "UCSF ChimeraX: Structure visualization for researchers, educators, and developers". Protein Science. 30 (1): 70–82. doi:10.1002/pro.3943. PMC 7737788. PMID 32881101.
^Toton E, Lisiak N, Sawicka P, Rybczynska M (August 2014). "Beclin-1 and its role as a target for anticancer therapy". Journal of Physiology and Pharmacology. 65 (4): 459–467. PMID 25179078.
^Modregger J, Schmidt AA, Ritter B, Huttner WB, Plomann M (February 2003). "Characterization of Endophilin B1b, a brain-specific membrane-associated lysophosphatidic acid acyl transferase with properties distinct from endophilin A1". The Journal of Biological Chemistry. 278 (6): 4160–4167. doi:10.1074/jbc.M208568200. PMID 12456676.
Further reading
Maruyama K, Sugano S (January 1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–174. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S (October 1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–156. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
Seki N, Ohira M, Nagase T, Ishikawa K, Miyajima N, Nakajima D, et al. (October 1997). "Characterization of cDNA clones in size-fractionated cDNA libraries from human brain". DNA Research. 4 (5): 345–349. doi:10.1093/dnares/4.5.345. PMID 9455484.
Howard L, Nelson KK, Maciewicz RA, Blobel CP (October 1999). "Interaction of the metalloprotease disintegrins MDC9 and MDC15 with two SH3 domain-containing proteins, endophilin I and SH3PX1". The Journal of Biological Chemistry. 274 (44): 31693–31699. doi:10.1074/jbc.274.44.31693. PMID 10531379.
Lai CH, Chou CY, Ch'ang LY, Liu CS, Lin W (May 2000). "Identification of novel human genes evolutionarily conserved in Caenorhabditis elegans by comparative proteomics". Genome Research. 10 (5): 703–713. doi:10.1101/gr.10.5.703. PMC 310876. PMID 10810093.
Modregger J, Schmidt AA, Ritter B, Huttner WB, Plomann M (February 2003). "Characterization of Endophilin B1b, a brain-specific membrane-associated lysophosphatidic acid acyl transferase with properties distinct from endophilin A1". The Journal of Biological Chemistry. 278 (6): 4160–4167. doi:10.1074/jbc.M208568200. PMID 12456676.
Lee SY, Wenk MR, Kim Y, Nairn AC, De Camilli P (January 2004). "Regulation of synaptojanin 1 by cyclin-dependent kinase 5 at synapses". Proceedings of the National Academy of Sciences of the United States of America. 101 (2): 546–551. Bibcode:2004PNAS..101..546L. doi:10.1073/pnas.0307813100. PMC 327184. PMID 14704270.
Karbowski M, Jeong SY, Youle RJ (September 2004). "Endophilin B1 is required for the maintenance of mitochondrial morphology". The Journal of Cell Biology. 166 (7): 1027–1039. doi:10.1083/jcb.200407046. PMC 2172012. PMID 15452144.
Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, et al. (October 2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–1178. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID 16189514. S2CID 4427026.
Takahashi Y, Karbowski M, Yamaguchi H, Kazi A, Wu J, Sebti SM, et al. (November 2005). "Loss of Bif-1 suppresses Bax/Bak conformational change and mitochondrial apoptosis". Molecular and Cellular Biology. 25 (21): 9369–9382. doi:10.1128/MCB.25.21.9369-9382.2005. PMC 1265816. PMID 16227588.
Masuda M, Takeda S, Sone M, Ohki T, Mori H, Kamioka Y, Mochizuki N (June 2006). "Endophilin BAR domain drives membrane curvature by two newly identified structure-based mechanisms". The EMBO Journal. 25 (12): 2889–2897. doi:10.1038/sj.emboj.7601176. PMC 1500852. PMID 16763557.
Lee JW, Jeong EG, Soung YH, Nam SW, Lee JY, Yoo NJ, Lee SH (August 2006). "Decreased expression of tumour suppressor Bax-interacting factor-1 (Bif-1), a Bax activator, in gastric carcinomas". Pathology. 38 (4): 312–315. doi:10.1080/00313020600820880. PMID 16916719. S2CID 25210386.
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PDB gallery
1x43: Solution structure of the SH3 domain of Endophilin B1 (Sh3g1b1)
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1x43: Solution structure of the SH3 domain of Endophilin B1 (Sh3g1b1)
