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词条 CBLB (gene)
释义

  1. Function

  2. Clinical significance

  3. Interactions

  4. References

  5. External links

  6. Further reading

{{Infobox_gene}}

CBL-B is an E3 ubiquitin-protein ligase that in humans is encoded by the CBLB gene.[1][2] CBLB is a member of the CBL gene family.

Function

CBL-B functions as a negative regulator of T-cell activation.[3] CBL-B expression in T cells causes ligand-induced T cell receptor down-modulation, controlling the activation degree of T cells during antigen presentation.[4][5]

Clinical significance

Mutation of the CBLB gene has been associated with autoimmune conditions such as type 1 diabetes.[6][7]

Interactions

CBLB has been shown to interact with:

  • CRKL,[8]
  • Epidermal growth factor receptor,[8][9]
  • Grb2,[10][11]
  • NEDD4,[12]
  • PIK3R1,[10][11] and
  • SH3KBP1.[13]

References

1. ^{{cite journal | vauthors = Keane MM, Rivero-Lezcano OM, Mitchell JA, Robbins KC, Lipkowitz S | title = Cloning and characterization of cbl-b: a SH3 binding protein with homology to the c-cbl proto-oncogene | journal = Oncogene | volume = 10 | issue = 12 | pages = 2367–77 |date=July 1995 | pmid = 7784085 | pmc = | doi = }}
2. ^{{cite web | title = Entrez Gene: CBLB Cas-Br-M (murine) ecotropic retroviral transforming sequence b| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=868| accessdate = }}
3. ^{{cite journal | vauthors = Wallner S, Gruber T, Baier G, Wolf D | title = Releasing the brake: targeting Cbl-b to enhance lymphocyte effector functions | journal = Clin. Dev. Immunol. | volume = 2012 | issue = | pages = 692639 | year = 2012 | pmid = 22550535 | pmc = 3328896 | doi = 10.1155/2012/692639 }}
4. ^{{cite journal | vauthors = Naramura M, Jang IK, Kole H, Huang F, Haines D, Gu H | title = Pc-Cbl and Cbl-b regulate T cell responsiveness by promoting ligand-induced TCR down-modulation. | journal = Nature Immunology | volume = 3 | issue = 12 | pages = 1192–9 | date = August 2002 | pmid=12415267 | doi=10.1038/ni855}}
5. ^{{cite journal | vauthors = Karwacz K, Bricogne C, MacDonald D, Arce F, Bennett CL, Collins M, Escors D | title = PD-L1 co-stimulation contributes to ligand-induced T cell receptor down-modulation on CD8+ T cells | journal = EMBO Molecular Medicine | volume = 3 | issue = 10 | pages = 581–92 | date = August 2011 | pmid = 21739608 | doi = 10.1002/emmm.201100165 | pmc=3191120}}
6. ^{{cite journal | vauthors = Hoyne GF, Flening E, Yabas M, Teh C, Altin JA, Randall K, Thien CB, Langdon WY, Goodnow CC | title = Visualizing the role of Cbl-b in control of islet-reactive CD4 T cells and susceptibility to type 1 diabetes | journal = J. Immunol. | volume = 186 | issue = 4 | pages = 2024–32 |date=February 2011 | pmid = 21248249 | doi = 10.4049/jimmunol.1002296}}
7. ^{{cite journal | vauthors = Yokoi N, Fujiwara Y, Wang HY, Kitao M, Hayashi C, Someya T, Kanamori M, Oiso Y, Tajima N, Yamada Y, Seino Y, Ikegami H, Seino S | title = Identification and functional analysis of CBLB mutations in type 1 diabetes | journal = Biochem. Biophys. Res. Commun. | volume = 368 | issue = 1 | pages = 37–42 |date=March 2008 | pmid = 18201552 | doi = 10.1016/j.bbrc.2008.01.032 }}
8. ^{{cite journal | vauthors = Schulze WX, Deng L, Mann M | title = Phosphotyrosine interactome of the ErbB-receptor kinase family | journal = Mol. Syst. Biol. | volume = 1 | issue = | pages = 2005.0008 | year = 2005 | pmid = 16729043 | pmc = 1681463 | doi = 10.1038/msb4100012 }}
9. ^{{cite journal | vauthors = Ettenberg SA, Keane MM, Nau MM, Frankel M, Wang LM, Pierce JH, Lipkowitz S | title = cbl-b inhibits epidermal growth factor receptor signaling | journal = Oncogene | volume = 18 | issue = 10 | pages = 1855–66 |date=March 1999 | pmid = 10086340 | doi = 10.1038/sj.onc.1202499 }}
10. ^{{cite journal | vauthors = Elly C, Witte S, Zhang Z, Rosnet O, Lipkowitz S, Altman A, Liu YC | title = Tyrosine phosphorylation and complex formation of Cbl-b upon T cell receptor stimulation | journal = Oncogene | volume = 18 | issue = 5 | pages = 1147–56 |date=February 1999 | pmid = 10022120 | doi = 10.1038/sj.onc.1202411 }}
11. ^{{cite journal | vauthors = Lavagna-Sévenier C, Marchetto S, Birnbaum D, Rosnet O | title = The CBL-related protein CBLB participates in FLT3 and interleukin-7 receptor signal transduction in pro-B cells | journal = J. Biol. Chem. | volume = 273 | issue = 24 | pages = 14962–7 |date=June 1998 | pmid = 9614102 | doi = 10.1074/jbc.273.24.14962 }}
12. ^{{cite journal | vauthors = Magnifico A, Ettenberg S, Yang C, Mariano J, Tiwari S, Fang S, Lipkowitz S, Weissman AM | title = WW domain HECT E3s target Cbl RING finger E3s for proteasomal degradation | journal = J. Biol. Chem. | volume = 278 | issue = 44 | pages = 43169–77 |date=October 2003 | pmid = 12907674 | doi = 10.1074/jbc.M308009200 }}
13. ^{{cite journal | vauthors = Szymkiewicz I, Kowanetz K, Soubeyran P, Dinarina A, Lipkowitz S, Dikic I | title = CIN85 participates in Cbl-b-mediated down-regulation of receptor tyrosine kinases | journal = J. Biol. Chem. | volume = 277 | issue = 42 | pages = 39666–72 |date=October 2002 | pmid = 12177062 | doi = 10.1074/jbc.M205535200 }}

External links

  • {{UCSC gene info|CBLB}}

Further reading

{{refbegin | 2}}
  • {{cite book | vauthors=Fang N, Fang D, Wang HY, etal |veditors=Altman A |chapter=Regulation of immune responses by E3 ubiquitin-protein ligases |title=Signal Transduction Pathways in Autoimmunity |series=Current Directions in Autoimmunity |volume=5 |pages=161–75 |year=2002 |pmid=11826757 |doi=10.1159/000060552 |isbn=3-8055-7308-1}}
  • {{cite journal | vauthors=Ohira M, Morohashi A, Nakamura Y |title=Neuroblastoma oligo-capping cDNA project: toward the understanding of the genesis and biology of neuroblastoma |journal=Cancer Lett. |volume=197 |issue= 1–2 |pages= 63–8 |year= 2003 |pmid= 12880961 |doi=10.1016/S0304-3835(03)00085-5 |display-authors=etal}}
  • {{cite journal | vauthors=Bonaldo MF, Lennon G, Soares MB |title=Normalization and subtraction: two approaches to facilitate gene discovery |journal=Genome Res. |volume=6 |issue= 9 |pages= 791–806 |year= 1997 |pmid= 8889548 |doi=10.1101/gr.6.9.791 }}
  • {{cite journal | vauthors=Bustelo XR, Crespo P, López-Barahona M |title=Cbl-b, a member of the Sli-1/c-Cbl protein family, inhibits Vav-mediated c-Jun N-terminal kinase activation |journal=Oncogene |volume=15 |issue= 21 |pages= 2511–20 |year= 1997 |pmid= 9399639 |doi=10.1038/sj.onc.1201430 |display-authors=etal}}
  • {{cite journal | vauthors=Lavagna-Sévenier C, Marchetto S, Birnbaum D, Rosnet O |title=The CBL-related protein CBLB participates in FLT3 and interleukin-7 receptor signal transduction in pro-B cells |journal=J. Biol. Chem. |volume=273 |issue= 24 |pages= 14962–7 |year= 1998 |pmid= 9614102 |doi=10.1074/jbc.273.24.14962 }}
  • {{cite journal | vauthors=Elly C, Witte S, Zhang Z |title=Tyrosine phosphorylation and complex formation of Cbl-b upon T cell receptor stimulation |journal=Oncogene |volume=18 |issue= 5 |pages= 1147–56 |year= 1999 |pmid= 10022120 |doi= 10.1038/sj.onc.1202411 |display-authors=etal}}
  • {{cite journal | vauthors=Zhang Z, Elly C, Qiu L |title=A direct interaction between the adaptor protein Cbl-b and the kinase zap-70 induces a positive signal in T cells |journal=Curr. Biol. |volume=9 |issue= 4 |pages= 203–6 |year= 1999 |pmid= 10074432 |doi=10.1016/S0960-9822(99)80090-6 |display-authors=etal}}
  • {{cite journal | vauthors=Ettenberg SA, Keane MM, Nau MM |title=cbl-b inhibits epidermal growth factor receptor signaling |journal=Oncogene |volume=18 |issue= 10 |pages= 1855–66 |year= 1999 |pmid= 10086340 |doi= 10.1038/sj.onc.1202499 |display-authors=etal}}
  • {{cite journal | vauthors=Wong ES, Lim J, Low BC |title=Evidence for direct interaction between Sprouty and Cbl |journal=J. Biol. Chem. |volume=276 |issue= 8 |pages= 5866–75 |year= 2001 |pmid= 11053437 |doi= 10.1074/jbc.M006945200 |display-authors=etal}}
  • {{cite journal | vauthors=Fang D, Wang HY, Fang N |title=Cbl-b, a RING-type E3 ubiquitin ligase, targets phosphatidylinositol 3-kinase for ubiquitination in T cells |journal=J. Biol. Chem. |volume=276 |issue= 7 |pages= 4872–8 |year= 2001 |pmid= 11087752 |doi= 10.1074/jbc.M008901200 |display-authors=etal}}
  • {{cite journal | vauthors=Ettenberg SA, Magnifico A, Cuello M |title=Cbl-b-dependent coordinated degradation of the epidermal growth factor receptor signaling complex |journal=J. Biol. Chem. |volume=276 |issue= 29 |pages= 27677–84 |year= 2001 |pmid= 11375397 |doi= 10.1074/jbc.M102641200 |display-authors=etal}}
  • {{cite journal | vauthors=Arron JR, Vologodskaia M, Wong BR |title=A positive regulatory role for Cbl family proteins in tumor necrosis factor-related activation-induced cytokine (trance) and CD40L-mediated Akt activation |journal=J. Biol. Chem. |volume=276 |issue= 32 |pages= 30011–7 |year= 2001 |pmid= 11406619 |doi= 10.1074/jbc.M100414200 |display-authors=etal}}
  • {{cite journal | vauthors=Fang D, Liu YC |title=Proteolysis-independent regulation of PI3K by Cbl-b-mediated ubiquitination in T cells |journal=Nat. Immunol. |volume=2 |issue= 9 |pages= 870–5 |year= 2001 |pmid= 11526404 |doi= 10.1038/ni0901-870 }}
  • {{cite journal | vauthors=Sattler M, Pride YB, Quinnan LR |title=Differential expression and signaling of CBL and CBL-B in BCR/ABL transformed cells |journal=Oncogene |volume=21 |issue= 9 |pages= 1423–33 |year= 2002 |pmid= 11857085 |doi= 10.1038/sj.onc.1205202 |display-authors=etal}}
  • {{cite journal | vauthors=Yasuda T, Tezuka T, Maeda A |title=Cbl-b positively regulates Btk-mediated activation of phospholipase C-gamma2 in B cells |journal=J. Exp. Med. |volume=196 |issue= 1 |pages= 51–63 |year= 2002 |pmid= 12093870 |doi=10.1084/jem.20020068 | pmc=2194016 |display-authors=etal}}
  • {{cite journal | vauthors=Szymkiewicz I, Kowanetz K, Soubeyran P |title=CIN85 participates in Cbl-b-mediated down-regulation of receptor tyrosine kinases |journal=J. Biol. Chem. |volume=277 |issue= 42 |pages= 39666–72 |year= 2002 |pmid= 12177062 |doi= 10.1074/jbc.M205535200 |display-authors=etal}}
  • {{cite journal | vauthors=Haglund K, Shimokawa N, Szymkiewicz I, Dikic I |title=Cbl-directed monoubiquitination of CIN85 is involved in regulation of ligand-induced degradation of EGF receptors |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 19 |pages= 12191–6 |year= 2002 |pmid= 12218189 |doi= 10.1073/pnas.192462299 | pmc=129420 }}
  • {{cite journal | vauthors=Strausberg RL, Feingold EA, Grouse LH |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 | pmc=139241 |display-authors=etal}}
{{refend}}{{PDB Gallery|geneid=868}}
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