Genetics of Alzheimer's Disease and Frontotemporal Dementia.
Florence, Italy. In Curr Mol Med, 10 Nov 2014
Up to now, the genetics of familial forms of FTD is related to 7 genes: the microtubule-associated protein tau (MAPT) progranulin (GRN), the valosin-containing protein (VCP), chromatin-modifying 2B (CHMP2B), the TARDNA binding protein 43 encoding gene (TARBDP), fused in sarcoma (FUS) and the last hexanucleotide expansion repeats in the open reading frame of chromosome 9 (C9orf72).
Immunohistochemical Analysis of Expressions of RB1, CDK4, HSP90, cPLA2G4A, and CHMP2B Is Helpful in Distinction between Myxofibrosarcoma and Myxoid Liposarcoma.
Pittsburgh, United States. In Int J Surg Pathol, 31 Oct 2014
The role and diagnostic efficacy of gene and protein products RB1, CDK4, CHMP2B, HSP90, and cPLA2G4A, all previously shown to be involved in tumor genesis and cell proliferation, were examined by immunohistochemical techniques in 32 cases of myxofibrosarcomas and 29 myxoid liposarcomas (all diagnosis had been confirmed by fluorescence in situ hybridization).
Parkinsonian syndrome in familial frontotemporal dementia.
Katowice, Poland. In Parkinsonism Relat Disord, 30 Sep 2014
Since then, mutations in several other genes have been identified for FTD with parkinsonism, including chromosome 9 open reading frame 72 (C9ORF72), chromatin modifying protein 2B (CHMP2B), valosin-containing protein (VCP), fused in sarcoma (FUS) and transactive DNA-binding protein (TARDBP).
Identify mutation in amyotrophic lateral sclerosis cases using HaloPlex target enrichment system.
Shanghai, China. In Neurobiol Aging, Aug 2014
We performed this approach to screen 18 causative genes of ALS, including SOD1, SETX, FUS, ANG, TARDBP, ALS2, FIG4, VAPB, OPTN, DAO, VCP, UBQLN2, SPG11, SIGMAR1, DCTN1, SQSTM1, PFN1, and CHMP2B in 8 ALS probands.
Atrogin-1 deficiency promotes cardiomyopathy and premature death via impaired autophagy.
In J Clin Invest, Jul 2014
Here, using atrogin-1 KO mice in combination with in vivo pulsed stable isotope labeling of amino acids in cell culture proteomics and biochemical and cellular analyses, we identified charged multivesicular body protein 2B (CHMP2B), which is part of an endosomal sorting complex (ESCRT) required for autophagy, as a target of atrogin-1-mediated degradation.
A novel GRN mutation (GRN c.708+6_+9delTGAG) in frontotemporal lobar degeneration with TDP-43-positive inclusions: clinicopathologic report of 6 cases.
Jacksonville, United States. In J Neuropathol Exp Neurol, May 2014
Mutations in 7 known genes (MAPT, GRN, C9orf72, VCP, CHMP2B, and, rarely, TARDBP and FUS) are associated with frontotemporal dementia, and the pathologic classification of frontotemporal lobar degeneration has recently been modified to reflect these discoveries.
CK2 involvement in ESCRT-III complex phosphorylation.
Padova, Italy. In Arch Biochem Biophys, Apr 2014
Here we show that protein kinase CK2α is involved in the phosphorylation of the ESCRT-III subunits CHMP3 and CHMP2B, as well as of VPS4B/SKD1, an ATPase that mediates ESCRT-III disassembly.
[The genetics of corticobasal syndrome].
Yokohama, Japan. In Brain Nerve, 2013
FTLD is also associated with VCP, CHMP2B, TARDBP and FUS mutations, but each of these account for <1% of familial FTLD cases.
Mouse models of frontotemporal dementia.
Birmingham, United States. In Ann Neurol, 2012
MAPT/tau, GRN/progranulin, and C9ORF72 have emerged as common FTD genes, and TARDBP/TDP-43, VCP, FUS, and CHMP2B have been identified as less common genetic causes.
Frontotemporal dementia caused by CHMP2B mutations.
London, United Kingdom. In Curr Alzheimer Res, 2011
recent advances in our understanding of the molecular basis of CHMP2B mutations indicate that the mechanisms involved may be broadly relevant to neurodegenerative processes.[review]
ESCRT-III recognition by VPS4 ATPases.
Salt Lake City, United States. In Nature, 2007
Structures of VPS4A MIT-CHMP1A and VPS4B MIT-CHMP2B complexes reveal that the C-terminal CHMP motif forms an amphipathic helix that binds in a groove between the last two helices of the tetratricopeptide-like repeat (TPR) of the VPS4 MIT domain, but in the opposite orientation to that of a canonical TPR interaction.