SH3GLB1

SH3GLB1
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1X43
Identifiers
Aliases	SH3GLB1, Bif-1, PPP1R70, dJ612B15.2, CGI-61, SH3 domain containing GRB2 like endophilin B1, SH3 domain containing GRB2 like, endophilin B1
External IDs	OMIM: 609287; MGI: 1859730; HomoloGene: 9337; GeneCards: SH3GLB1; OMA:SH3GLB1 - orthologs
Gene location (Human) Chr. Chromosome 1 (human)[1] Band 1p22.3 Start 86,704,570 bp[1] End 86,748,184 bp[1]
Gene location (Mouse) Chr. Chromosome 3 (mouse)[2] Band 3|3 H2 Start 144,389,439 bp[2] End 144,426,096 bp[2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in tibialis anterior muscle deltoid muscle right ventricle muscle of trunk Skeletal muscle tissue of rectus abdominis gastrocnemius muscle thoracic diaphragm oocyte muscle of arm biceps brachii Top expressed in blood seminiferous tubule ankle endothelial cell of lymphatic vessel temporal muscle digastric muscle sternocleidomastoid muscle triceps brachii muscle medial head of gastrocnemius muscle right ventricle More reference expression data BioGPS More reference expression data
Gene ontology Molecular function protein homodimerization activity protein binding identical protein binding lipid binding cadherin binding Cellular component cytoplasm Golgi apparatus membrane Golgi membrane mitochondrial outer membrane autophagosome membrane midbody mitochondrion extracellular exosome cytoplasmic vesicle cytosol Biological process cellular response to glucose starvation regulation of cytokinesis regulation of protein stability positive regulation of autophagosome assembly positive regulation of autophagy positive regulation of protein targeting to mitochondrion cellular response to amino acid starvation receptor catabolic process autophagy protein complex oligomerization membrane fission positive regulation of protein oligomerization positive regulation of membrane tubulation autophagic cell death regulation of macroautophagy protein localization to vacuolar membrane apoptotic process Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 51100 54673 Ensembl ENSG00000097033 ENSMUSG00000037062 UniProt Q9Y371 Q9JK48 RefSeq (mRNA) NM_001206651 NM_001206652 NM_001206653 NM_016009 NM_001282037 NM_001282042 NM_019464 NM_001379170 NM_001379171 NM_001379172 NM_001379173 NM_001379174 RefSeq (protein) NP_001193580 NP_001193581 NP_001193582 NP_057093 NP_001268966 NP_001268971 NP_062337 NP_001366099 NP_001366100 NP_001366101 NP_001366102 NP_001366103 Location (UCSC) Chr 1: 86.7 – 86.75 Mb Chr 3: 144.39 – 144.43 Mb PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

Endophilin-B1 is a protein that in humans is encoded by the SH3GLB1 gene.[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

1. GRCh38: Ensembl release 89: ENSG00000097033 – Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000037062 – Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. Pierrat 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.
6. Cuddeback 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.
7. "Entrez Gene: SH3GLB1 SH3-domain GRB2-like endophilin B1".
8. 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.
9. 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.
10. 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.
11. 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.
12. Coppola D, Oliveri C, Sayegh Z, Boulware D, Takahashi Y, Pow-Sang J, et al. (September 2008). "Bax-interacting factor-1 expression in prostate cancer". Clinical Genitourinary Cancer. 6 (2): 117–121. doi:10.3816/CGC.2008.n.018. PMC 2626142. PMID 18824435.
13. 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.
14. Bhatt 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.
15. 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.
16. 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.
17. 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.