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SH3GLB1

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SH3GLB1
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesSH3GLB1, Bif-1, PPP1R70, dJ612B15.2, CGI-61, SH3 domain containing GRB2 like endophilin B1, SH3 domain containing GRB2 like, endophilin B1
External IDsOMIM: 609287; MGI: 1859730; HomoloGene: 9337; GeneCards: SH3GLB1; OMA:SH3GLB1 - orthologs
Orthologs
SpeciesHumanMouse
Entrez

51100

54673

Ensembl

ENSG00000097033

ENSMUSG00000037062

UniProt

Q9Y371

Q9JK48

RefSeq (mRNA)

NM_001206651
NM_001206652
NM_001206653
NM_016009

RefSeq (protein)

NP_001193580
NP_001193581
NP_001193582
NP_057093

Location (UCSC)Chr 1: 86.7 – 86.75 MbChr 3: 144.39 – 144.43 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/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

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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

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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

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  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000097033 – Ensembl, May 2017
  2. ^ a b c 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. ^ a b c 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. ^ a b 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. ^ a b 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

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