ESCRT-1
MVB12A
https://www.ncbi.nlm.nih.gov/gene/93343- Also known as CFBP; FAM125A
- Expression Ubiquitous expression in ovary (RPKM 33.5), adrenal (RPKM 16.5) and 24 other tissues See more Orthologs mouse a
Preferred Names
- multivesicular body subunit 12A
- Names
- CIN85/CD2AP family binding protein, (CFBP)
- ESCRT-I complex subunit MVB12A
- family with sequence similarity 125, member A
Peptide sequence, Isoform 2, transkript 2; 1-181 a.a.
https://www.ncbi.nlm.nih.gov/protein/NP_001291476.1Related articles in PubMed
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CFBP
is a novel tyrosine-phosphorylated protein that might function as a
regulator of CIN85/CD2AP. Konishi H, et al. J Biol
Chem, 2006 Sep 29. PMID 16895919
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The
molecular basis for selective assembly of the UBAP1-containing
endosome-specific ESCRT-I complex. Wunderley L, et al.
J Cell Sci, 2014 Feb 1. PMID 24284069, Free
PMC Article
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Structural basis for membrane targeting by the MVB12-associated β-prism domain of the human ESCRT-I MVB12 subunit. Boura E, et al. Proc Natl Acad Sci U S A, 2012 Feb 7. PMID 22232651, Free PMC Article
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Distinct functions of human MVB12A and MVB12B in the ESCRT-I dependent on their posttranslational modifications. Tsunematsu T, et al. Biochem Biophys Res Commun, 2010 Aug 20. PMID 20654576
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Human
ESCRT and ALIX proteins interact with proteins of the midbody and
function in cytokinesis. Morita E, et al. EMBO J, 2007
Oct 3. PMID 17853893, Free
PMC Article
See citations in PubMed for homologs of this gene provided by HomoloGene
GeneRIFs: Gene References Into FunctionsWhat's a GeneRIF?
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Key words.
CFBP is CIN85/CD2AP family binding protein
(CFBP recruiting Cbl to CIN85)
Decipher the global
network of the epidermal growth factor (EGF) receptor-mediated
signaling pathway, a large scale proteomic analysis of
tyrosine-phosphorylated proteins was conducted. Here, we focus on
characterizing a novel protein, CFBP (CIN85/CD2AP family
binding protein), identified in the study. CFBP was found to be
phosphorylated at tyrosine 204 upon EGF stimulation, and the
CIN85/CD2AP family was identified as a binding partner.
A proline-rich motif of CFBP is recognized by one of the three Src-homology 3 domains of CIN85/CD2AP, and the affinity of the interaction is regulated by the tyrosine phosphorylation of CFBP. They co-localize in actin enriched structures, and overexpression of CFBP induced morphological changes with actin reorganization.
Furthermore, CFBP accelerated the EGF receptor's down-regulation by facilitating the recruitment of Cbl to the CD2AP/CIN85 complex. Two spliced variants of CFBP lacking either exon 5 or 8 are also expressed, and the variant lacking exon 5 without the proline-rich motif lacks the ability to bind to the CIN85/CD2AP family. The CFBP protein seems to play a key role in the ligand-mediated internalization and down-regulation of the EGF receptor.
https://www.ncbi.nlm.nih.gov/pubmed/16895919/A proline-rich motif of CFBP is recognized by one of the three Src-homology 3 domains of CIN85/CD2AP, and the affinity of the interaction is regulated by the tyrosine phosphorylation of CFBP. They co-localize in actin enriched structures, and overexpression of CFBP induced morphological changes with actin reorganization.
Furthermore, CFBP accelerated the EGF receptor's down-regulation by facilitating the recruitment of Cbl to the CD2AP/CIN85 complex. Two spliced variants of CFBP lacking either exon 5 or 8 are also expressed, and the variant lacking exon 5 without the proline-rich motif lacks the ability to bind to the CIN85/CD2AP family. The CFBP protein seems to play a key role in the ligand-mediated internalization and down-regulation of the EGF receptor.
What is CIN85?
https://www.google.se/search?q=Cbl+recruitment+to+CIN85++by+MVB12A&source=lnms&tbm=isch&sa=X&ved=0ahUKEwjX67SvjY_bAhXGIpoKHfNYCCUQ_AUICygC&biw=1024&bih=471&dpr=1.88#imgdii=g3d3TQeDdieEnM:&imgrc=iZi13VzzNMNVdM:
https://www.ncbi.nlm.nih.gov/pubmed/27353366
Format: Abstract Sci Signal. 2016 Jun 28;9(434):ra66. doi: 10.1126/scisignal.aad6275.
The adaptor protein CIN85 assembles intracellular signaling clusters for B cell activation.
Kühn
J1, Wong
LE2, Pirkuliyeva
S1, Schulz
K1, Schwiegk
C2, Fünfgeld
KG3, Keppler
S4, Batista
FD4, Urlaub
H5, Habeck
M6, Becker
S2, Griesinger
C7, Wienands
J8. Abstract
The adaptor
molecule Cbl-interacting protein of 85 kD (CIN85) regulates
signaling from a number of cell surface receptors, such as growth
factor receptors and antigen receptors on lymphocytes. Because of its
multidomain structure, CIN85 is thought to act as a classical adaptor
protein that connects functionally distinct components of a given
signaling pathway through diverse protein domains.
However, we found
that in B lymphocytes, CIN85 functions to oligomerize SLP-65,
which is the central effector protein of the B cell receptor (BCR).
Therefore, CIN85 trimerizes through a carboxyl-terminal,
coiled-coil domain. The multiple Src homology 3 (SH3) domains of
trimeric CIN85 molecules associated with multiple SLP-65 molecules,
which recruited further CIN85 trimers, thereby perpetuating the
oligomerization process. Formation of this oligomeric signaling
complex in resting B cells rendered the cells poised for the
efficient initiation of intracellular signaling upon BCR stimulation.
Our data suggest that the functionality of signaling cascades does
not rely solely on the qualitative linkage of their various
components but requires a critical number of effectors to become
concentrated in signaling complexes.
- PMID: 27353366 DOI: 10.1126/scisignal.aad6275 [Indexed for MEDLINE]
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