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Bardet-Biedl syndrome 4

This gene is a member of the Bardet-Biedl syndrome (BBS) gene family. Bardet-Biedl syndrome is an autosomal recessive disorder characterized by severe pigmentary retinopathy, obesity, polydactyly, renal malformation and mental retardation. The proteins encoded by BBS gene family members are structurally diverse. The similar phenotypes exhibited by mutations in BBS gene family members are likely due to the protein's shared roles in cilia formation and function. Many BBS proteins localize to the basal bodies, ciliary axonemes, and pericentriolar regions of cells. BBS proteins may also be involved in intracellular trafficking via microtubule-related transport. The protein encoded by this gene has sequence similarity to O-linked N-acetylglucosamine (O-GlcNAc) transferases in plants and archaebacteria and in human forms a multi-protein "BBSome" complex with six other BBS proteins. Alternative splice variants have been described but their predicted protein products have not been experimentally verified.[provided by RefSeq, Jan 2009] (from NCBI)
Top mentioned proteins: BBS, BBS1, Kms, BBS7, BBS8
Papers on BBS4
Differential effects on β-cell mass by disruption of Bardet-Biedl syndrome or Alstrom syndrome genes.
Zaghloul et al., Baltimore, United States. In Hum Mol Genet, Feb 2016
Loss of the Alstrom gene, alms1, resulted in a significant decrease in β-cell production whereas loss of BBS genes, bbs1 or bbs4, resulted in a significant increase.
Targeted multi-gene panel testing for the diagnosis of Bardet Biedl syndrome: Identification of nine novel mutations across BBS1, BBS2, BBS4, BBS7, BBS9, BBS10 genes.
Ozkinay et al., İzmir, Turkey. In Eur J Med Genet, Dec 2015
In this study, 15 patients with clinically diagnosed BBS were investigated using a next generation sequencing panel which included 17 known BBS causing genes (BBS1, BBS2, ARL6, BBS4, BBS5, MKKS, BBS7, TTC8, BBS9, BBS10, TRIM32, BBS12, MKS1, NPHP6, WDPCP, SDCCAG8, NPHP1).
Architectures of multisubunit complexes revealed by a visible immunoprecipitation assay using fluorescent fusion proteins.
Nakayama et al., Kyoto, Japan. In J Cell Sci, Jul 2015
We also demonstrated the assembly sequence of the BBSome around the centrosome, and showed that BBS18 (also known as BBIP1 and BBIP10) serves as a linker between BBS4 and BBS8 (also known as TTC8).
BBS4 and BBS5 show functional redundancy in the BBSome to regulate the degradative sorting of ciliary sensory receptors.
Hu et al., Rochester, United States. In Sci Rep, 2014
BBS-4 directly interacts with BBS-5 and the interaction can be disrupted by a conserved mutation identified in human BBS4.
Bardet-Biedl syndrome proteins 1 and 3 regulate the ciliary trafficking of polycystic kidney disease 1 protein.
Zhou et al., Boston, United States. In Hum Mol Genet, 2014
Here, we demonstrate that, unlike the seven-span somatostatin receptor 3 or the leptin receptor that interacts with all subunits of the BBSome, the ADPKD protein polycystin-1 (PC1) interacts with BBS1, BBS4, BBS5 and BBS8, four of the seven components of the BBSome.
BBS4 is necessary for ciliary localization of TrkB receptor and activation by BDNF.
Zaghloul et al., Baltimore, United States. In Plos One, 2013
Upon loss of BBS4 expression in cultured cells, we observed decreased phosphorylation and activation by BDNF of its target receptor, TrkB.
A novel nonsense mutation in BBS4 gene identified in a Chinese family with Bardet-Biedl syndrome.
Peng et al., Beijing, China. In Chin Med J (engl), 2013
RESULTS: We identified a novel homozygous nonsense mutation (c.70A>T, p.K24X) in the BBS4 gene exon 2 in the proband.
Autophagy promotes primary ciliogenesis by removing OFD1 from centriolar satellites.
Zhong et al., Dallas, United States. In Nature, 2013
In autophagy-deficient Atg5 or Atg3 null mouse embryonic fibroblasts, OFD1 accumulates at centriolar satellites, leading to fewer and shorter primary cilia and a defective recruitment of BBS4 (Bardet-Biedl syndrome 4) to cilia.
Exome capture sequencing identifies a novel mutation in BBS4.
Chen et al., Houston, United States. In Mol Vis, 2010
A novel missense mutation in BBS4 that co-segregates with Leber Congenital Amaurosis was identified in a consanguineous family from Saudi Arabia.
Requirement of Bardet-Biedl syndrome proteins for leptin receptor signaling.
Sheffield et al., United States. In Hum Mol Genet, 2009
Bardet-Biedl syndrome (BBS) proteins mediate LepR trafficking and that impaired LepR signaling underlies energy imbalance in BBS.
Bardet-Biedl syndrome proteins are required for the localization of G protein-coupled receptors to primary cilia.
Mykytyn et al., Columbus, United States. In Proc Natl Acad Sci U S A, 2008
a lack of ciliary localization of somatostatin receptor type 3 (Sstr3) and melanin-concentrating hormone receptor 1 (Mchr1) in neurons from mice lacking the Bbs2 or Bbs4 gene
Loss of Bardet-Biedl syndrome proteins alters the morphology and function of motile cilia in airway epithelia.
Welsh et al., Iowa City, United States. In Proc Natl Acad Sci U S A, 2008
Although BBS proteins were not required for ciliogenesis, their loss caused structural defects in a fraction of cilia covering mouse airway epithelia in Bbs1, Bbs2, Bbs4, and Bbs6 mutant mice.
Loss of Bardet Biedl syndrome proteins causes defects in peripheral sensory innervation and function.
Katsanis et al., Baltimore, United States. In Proc Natl Acad Sci U S A, 2007
ablation of BBS1 and BBS4 leads to alterations of s.c. sensory innervation and trafficking of the thermosensory channel TRPV1 and the mechanosensory channel STOML3
Disruption of the basal body compromises proteasomal function and perturbs intracellular Wnt response.
Katsanis et al., Baltimore, United States. In Nat Genet, 2007
Here we show that bbs1, bbs4 and mkks (also known as bbs6), which encode basal body proteins, are required for convergence and extension in zebrafish and interact with wnt11 and wnt5b.
[Update on Bardet-Biedl syndrome].
Mandel et al., Strasbourg, France. In J Fr Ophtalmol, 2005
To date, six different genes have been identified: BBS1, BBS2, BBS4, BBS6, BBS7 and BBS8.
Use of isolated populations in the study of a human obesity syndrome, the Bardet-Biedl syndrome.
Sheffield, Iowa City, United States. In Pediatr Res, 2004
The predicted BBS1, BBS2, BBS4, BBS7, and BBS8 gene products do not seem to be molecular chaperones, on the basis of a lack of sequence similarity to the chaperonin family of proteins.
The Bardet-Biedl protein BBS4 targets cargo to the pericentriolar region and is required for microtubule anchoring and cell cycle progression.
Beales et al., Canada. In Nat Genet, 2004
BBS4 is one of several proteins that cause Bardet-Biedl syndrome (BBS), a multisystemic disorder of genetic and clinical complexity.
Bardet-Biedl Syndrome
Beales et al., Seattle, United States. In Unknown Journal, 2003
At least 19 genes are associated with BBS: BBS1, BBS2, ARL6 (BBS3), BBS4, BBS5, MKKS (BBS6), BBS7, TTC8 (BBS8), BBS9, BBS10, TRIM32 (BBS11), BBS12, MKS1 (BBS13), CEP290 (BBS14), WDPCP (BBS15), SDCCAG8 (BBS16), LZTFL1 (BBS17), BBIP1 (BBS18), and IFT27 (BBS19).
Identification of the gene (BBS1) most commonly involved in Bardet-Biedl syndrome, a complex human obesity syndrome.
Sheffield et al., Iowa City, United States. In Nat Genet, 2002
q23 (BBS4), 2q31 (BBS5) and 20p12 (BBS6).
Identification of the gene that, when mutated, causes the human obesity syndrome BBS4.
Sheffield et al., Iowa City, United States. In Nat Genet, 2001
(BBS4), 2q31 (BBS5), and 20p12 (BBS6).
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