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We identified a novel H395R substitution in MKKS/BBS6 that results in a unique phenotype of only retinitis pigmentosa and polydactyly.
we report here, for the first time, in Indian population, a novel, different profile of mutations in BBS (show BBS2 Proteins) genes (BBS3, BBS9 (show BBS9 Proteins), BBS10 (show BBS10 Proteins) and BBS2 (show BBS2 Proteins)) compared to worldwide (BBS1 (show BBS1 Proteins) and 10) reports.
Novel mutation (c.1272+1G>A) in BBS6 found in Tunisian families with Bardet-Biedl syndrome.
Findings indicate that Bbs (show BBS2 Proteins) proteins play a central role in the regulation of the actin cytoskeleton and control the cilia length through alteration of RhoA (show RHOA Proteins) levels.
Three uORFs (uMKKS0, uMKKS1 and uMKKS2) are reported, and they can repress the translation of the downstream MKKS ORF. uMKKS1 and uMKKS2 are highly conserved in mammals and they encode two different mitochondrial membrane proteins respectively.
Using sequence analysis, the role of BBS6, 10 and 12 was assessed in a Bardet-Biedl syndrome patient population comprising 93 cases from 74 families.
genetic variations at MKKS gene influence the risk of metabolic syndrome
The presence of three mutant alleles in the BBS (show BBS2 Proteins) family correlates with a more severe Bardet-Biedl phenotype.
MKKS/BBS6 is a novel centrosomal component required for cytokinesis
These results indicate that the MKKS mutants have an abnormal conformation and that chaperone-dependent degradation mediated by CHIP is a key feature of McKusick-Kaufman syndrome/Bardet-Biedl syndrome diseases.
Combinations of Cep290rd16 & Mkksko alleles improved ciliogenesis & sensory functions vs either mutant alone. Altered association of CEP290 & MKKS affects multiprotein complex integrity at the cilia transition zone & basal body.
Data implicate Bardet-Biedl syndrome genes in the regulation of vascular function and demonstrate that disrupting Bbs2 (show BBS2 Proteins) and Bbs6 genes affect differentially the vascular function.
Mutations in Mkks are the basis of the BBS (show BBS2 Proteins)-like syndrome in knockout mice.
Although BBS (show BBS2 Proteins) proteins were not required for ciliogenesis, their loss caused structural defects in a fraction of cilia covering mouse airway epithelia in Bbs1 (show BBS1 Proteins), Bbs2 (show BBS2 Proteins), Bbs4 (show BBS4 Proteins), and Bbs6 mutant mice.
Bardet-Biedl syndrome (BBS (show BBS2 Proteins)) proteins mediate LepR (show LEPR Proteins) trafficking and that impaired LepR (show LEPR Proteins) signaling underlies energy imbalance in BBS (show BBS2 Proteins).
This gene encodes a protein which shares sequence similarity with other members of the chaperonin family. The encoded protein may have a role in protein folding, processing and assembly. Mutations in this gene have been observed in patients with Bardet-Biedl syndrome type 6 and McKusick-Kaufman syndrome. Alternative splicing results in multiple transcript variants.
McKusick-Kaufman syndrome protein
, McKusick-Kaufman/Bardet-Biedl syndromes putative chaperonin
, Bardet-Biedl syndrome 6
, McKusick-Kaufman syndrome
, mcKusick-Kaufman/Bardet-Biedl syndromes putative chaperonin-like
, McKusick-Kaufman/Bardet-Biedl syndromes putative chaperonin-like
, bardet-Biedl syndrome 6 protein
, McKusick-Kaufman syndrome protein; MKKS protein
, protein Bbs6 homolog