SH3GLB1

Last updated
SH3GLB1
Protein SH3GLB1 PDB 1x43.png
Available structures
PDB Ortholog search: PDBe RCSB
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
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
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 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.

Contents

Structure

A pseudo-atomic model of helical scaffolds formed by a truncated form of endophilin-B1. Based on a ChimeraX rendering of 6UP6. Endophilin-b1-helical-scaffold.png
A pseudo-atomic model of helical scaffolds formed by a truncated form of endophilin-B1. Based on a 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. [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]

Related Research Articles

<span class="mw-page-title-main">Apoptosis regulator BAX</span> Mammalian protein found in Homo sapiens

Apoptosis regulator BAX, also known as bcl-2-like protein 4, is a protein that in humans is encoded by the BAX gene. BAX is a member of the Bcl-2 gene family. BCL2 family members form hetero- or homodimers and act as anti- or pro-apoptotic regulators that are involved in a wide variety of cellular activities. This protein forms a heterodimer with BCL2, and functions as an apoptotic activator. This protein is reported to interact with, and increase the opening of, the mitochondrial voltage-dependent anion channel (VDAC), which leads to the loss in membrane potential and the release of cytochrome c. The expression of this gene is regulated by the tumor suppressor P53 and has been shown to be involved in P53-mediated apoptosis.

<span class="mw-page-title-main">BAR domain</span> Group of highly conserved protein dimerisation domains

In molecular biology, BAR domains are highly conserved protein dimerisation domains that occur in many proteins involved in membrane dynamics in a cell. The BAR domain is banana-shaped and binds to membrane via its concave face. It is capable of sensing membrane curvature by binding preferentially to curved membranes. BAR domains are named after three proteins that they are found in: Bin, Amphiphysin and Rvs.

<span class="mw-page-title-main">Amphiphysin</span> Protein-coding gene in the species Homo sapiens

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<span class="mw-page-title-main">Mitochondrial membrane transport protein</span>

Mitochondrial membrane transport proteins, also known as mitochondrial carrier proteins, are proteins which exist in the membranes of mitochondria. They serve to transport molecules and other factors, such as ions, into or out of the organelles. Mitochondria contain both an inner and outer membrane, separated by the inter-membrane space, or inner boundary membrane. The outer membrane is porous, whereas the inner membrane restricts the movement of all molecules. The two membranes also vary in membrane potential and pH. These factors play a role in the function of mitochondrial membrane transport proteins. There are 53 discovered human mitochondrial membrane transporters, with many others that are known to still need discovered.

<span class="mw-page-title-main">Adapter molecule crk</span> Protein-coding gene in the species Homo sapiens

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Phospholipase D<sub>1</sub> Protein-coding gene in the species Homo sapiens

Phospholipase D1 (PLD1) is an enzyme that in humans is encoded by the PLD1 gene, though analogues are found in plants, fungi, prokaryotes, and even viruses.

<span class="mw-page-title-main">BIN1</span> Protein-coding gene in Homo sapiens

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<span class="mw-page-title-main">SH3KBP1</span> Protein-coding gene in the species Homo sapiens

SH3 domain-containing kinase-binding protein 1 is an adaptor protein that in humans is encoded by the SH3KBP1 gene.

<span class="mw-page-title-main">DNM2</span> Protein-coding gene in the species Homo sapiens

Dynamin-2 is a protein that in humans is encoded by the DNM2 gene.

<span class="mw-page-title-main">DNM1</span> Protein-coding gene in the species Homo sapiens

Dynamin-1 is a protein that in humans is encoded by the DNM1 gene.

<span class="mw-page-title-main">SH3GL2</span> Protein-coding gene in the species Homo sapiens

Endophilin-A1 is a protein that in humans is encoded by the SH3GL2 gene.

<span class="mw-page-title-main">ADAM9</span> Protein-coding gene in the species Homo sapiens

Disintegrin and metalloproteinase domain-containing protein 9 is an enzyme that in humans is encoded by the ADAM9 gene.

<span class="mw-page-title-main">SH3GL3</span> Protein-coding gene in the species Homo sapiens

Endophilin-A3 is a protein that in humans is encoded by the SH3GL3 gene.

<span class="mw-page-title-main">SH3GL1</span> Protein-coding gene in the species Homo sapiens

Endophilin-A2 is a protein that in humans is encoded by the SH3GL1 gene.

<span class="mw-page-title-main">TOMM22</span> Protein-coding gene in the species Homo sapiens

Mitochondrial import receptor subunit TOM22 homolog is a protein that in humans is encoded by the TOMM22 gene.

<span class="mw-page-title-main">SH3BP5</span> Protein-coding gene in the species Homo sapiens

SH3 domain-binding protein 5 is a protein that in humans is encoded by the SH3BP5 gene.

<span class="mw-page-title-main">SGIP1</span> Protein-coding gene in the species Homo sapiens

SH3-containing GRB2-like protein 3-interacting protein 1 is a protein that in humans is encoded by the SGIP1 gene.

<span class="mw-page-title-main">MTCH1</span> Protein-coding gene in the species Homo sapiens

Mitochondrial carrier homolog 1 (MTCH1), also referred to as presenilin 1-associated protein (PSAP), is a protein that in humans is encoded by the MTCH1 gene on chromosome 6. MTCH1 is a proapoptotic mitochondrial protein potentially involved in Alzheimer’s disease (AD).

<span class="mw-page-title-main">POLRMT</span> Protein-coding gene in the species Homo sapiens

DNA-directed RNA polymerase, mitochondrial is an enzyme that in humans is encoded by the POLRMT gene.

<span class="mw-page-title-main">Rubicon (protein)</span> Human protein involved in autophagy regulation

Rubicon is a protein that in humans is encoded by the RUBCN gene. Rubicon is one of the few known negative regulators of autophagy, a cellular process that degrades unnecessary or damaged cellular components. Rubicon is recruited to its sites of action through interaction with the small GTPase Rab7, and impairs the autophagosome-lysosome fusion step of autophagy through inhibition of PI3KC3-C2.

References

  1. 1 2 3 GRCh38: Ensembl release 89: ENSG00000097033 - Ensembl, May 2017
  2. 1 2 3 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. 1 2 3 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. 1 2 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. 1 2 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