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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Dec 2016.

Charged multivesicular body protein 1B

CHMP1B, CHMP1.5, C18orf2, charged multivesicular body protein 1B
CHMP1B belongs to the chromatin-modifying protein/charged multivesicular body protein (CHMP) family. These proteins are components of ESCRT-III (endosomal sorting complex required for transport III), a complex involved in degradation of surface receptor proteins and formation of endocytic multivesicular bodies (MVBs). Some CHMPs have both nuclear and cytoplasmic/vesicular distributions, and one such CHMP, CHMP1A (MIM 164010), is required for both MVB formation and regulation of cell cycle progression (Tsang et al., 2006 [PubMed 16730941]).[supplied by OMIM, Mar 2008] (from NCBI)
Top mentioned proteins: Vps4, ATPase, Vps24, Vps60, BC2
Papers on CHMP1B
Structure and membrane remodeling activity of ESCRT-III helical polymers.
Frost et al., Salt Lake City, United States. In Science, Jan 2016
Here, we report the 4 angstrom resolution cryogenic electron microscopy reconstruction of a one-start, double-stranded helical copolymer composed of two different human ESCRT-III subunits, charged multivesicular body protein 1B (CHMP1B) and increased sodium tolerance 1 (IST1).
A network-based approach to identify disease-associated gene modules through integrating DNA methylation and gene expression.
Tuo et al., Xi'an, China. In Biochem Biophys Res Commun, Oct 2015
Importantly, through analyzing the functions and comparing expression and methylation values of these genes between cases and controls, we find some genes, such as VASN, SNRPD3, and gene modules, targeted by POLR2C, CHMP1B and TAF9, which might be novel breast cancer-related biomarkers.
A novel mechanism of regulating the ATPase VPS4 by its cofactor LIP5 and the endosomal sorting complex required for transport (ESCRT)-III protein CHMP5.
Xu et al., Ann Arbor, United States. In J Biol Chem, Apr 2015
The crystal structure of LIP5NTD in complex with the MIT (microtubule-interacting and transport)-interacting motifs of CHMP5 and a second ESCRT-III protein, CHMP1B, was determined at 1 Å resolution.
The endosomal protein CHARGED MULTIVESICULAR BODY PROTEIN1 regulates the autophagic turnover of plastids in Arabidopsis.
Otegui et al., Madison, United States. In Plant Cell, Feb 2015
Here, we show that the ESCRT-III subunit paralogs CHARGED MULTIVESICULAR BODY PROTEIN1 (CHMP1A) and CHMP1B are required for autophagic degradation of plastid proteins in Arabidopsis thaliana.
Interactions of the human LIP5 regulatory protein with endosomal sorting complexes required for transport.
Sundquist et al., Salt Lake City, United States. In J Biol Chem, 2013
We have investigated the biochemical and structural basis for different LIP5-ligand interactions and show that the first microtubule-interacting and trafficking (MIT) module of the tandem LIP5 MIT domain binds CHMP1B (and other ESCRT-III proteins) through canonical type 1 MIT-interacting motif (MIM1) interactions.
MITD1 is recruited to midbodies by ESCRT-III and participates in cytokinesis.
Blackstone et al., Bethesda, United States. In Mol Biol Cell, 2012
Here we assess comprehensively the ESCRT-III interactions of the MIT-domain family member MITD1 and identify strong interactions with charged multivesicular body protein 1B (CHMP1B), CHMP2A, and increased sodium tolerance-1 (IST1).
Calpain-7 binds to CHMP1B at its second α-helical region and forms a ternary complex with IST1.
Maki et al., Nagoya, Japan. In J Biochem, 2011
The interaction between CL7MIT and CHMP1B and between CL7MIT and IST1 became stronger when IST1 or CHMP1B was additionally coexpressed, suggesting formation of ternary complex of calpain-7, IST1 and CHMP1B.
Activation of human VPS4A by ESCRT-III proteins reveals ability of substrates to relieve enzyme autoinhibition.
Hanson et al., Saint Louis, United States. In J Biol Chem, 2010
Importantly, C-terminal fragments of all ESCRT-III proteins tested, including CHMP2A, CHMP1B, CHMP3, CHMP4A, CHMP6, and CHMP5, activated VPS4A suggesting that it disassembles ESCRT-III heteropolymers by affecting each component protein.
Structural basis for ESCRT-III protein autoinhibition.
Sundquist et al., Salt Lake City, United States. In Nat Struct Mol Biol, 2009
IST1 and its ESCRT-III binding partner, CHMP1B, both form higher-order helical structures in vitro, and IST1-CHMP1 interactions are required for abscission.
The ESCRT-related CHMP1A and B proteins mediate multivesicular body sorting of auxin carriers in Arabidopsis and are required for plant development.
Otegui et al., Madison, United States. In Plant Cell, 2009
Here, we show that the Arabidopsis thaliana ESCRT-related CHARGED MULTIVESICULAR BODY PROTEIN/CHROMATIN MODIFYING PROTEIN1A (CHMP1A) and CHMP1B proteins are essential for embryo and seedling development.
Structural basis for midbody targeting of spastin by the ESCRT-III protein CHMP1B.
Hurley et al., Bethesda, United States. In Nat Struct Mol Biol, 2008
The 2.5-A structure of the C-terminal tail of CHMP1B with the MIT domain of spastin reveals a specific, high-affinity complex involving a noncanonical binding site between the first and third helices of the MIT domain.
Human calpain 7/PalBH associates with a subset of ESCRT-III-related proteins in its N-terminal region and partly localizes to endocytic membrane compartments.
Maki et al., Nagoya, Japan. In J Biochem, 2008
In this study, we investigated the interactions of calpain 7 with all 11 ESCRT-III-related proteins, named charged multivesicular body proteins (CHMPs), and the subcellular localization of calpain 7. Pulldown assays using stable HEK293T transfectants of Strep-tagged calpain 7 revealed interactions of calpain 7 with a subset of FLAG-tagged CHMPs, among which CHMP1B was selected for further analyses.
Novel interactions of ESCRT-III with LIP5 and VPS4 and their implications for ESCRT-III disassembly.
Hanson et al., Saint Louis, United States. In Mol Biol Cell, 2008
Here we confirm that LIP5 binds tightly to CHMP5, but also find that it binds well to additional ESCRT-III proteins including CHMP1B, CHMP2A/hVps2-1, and CHMP3/hVps24 but not CHMP4A/hSnf7-1 or CHMP6/hVps20.
The MIT domain of UBPY constitutes a CHMP binding and endosomal localization signal required for efficient epidermal growth factor receptor degradation.
Urbé et al., Liverpool, United Kingdom. In J Biol Chem, 2007
UBPY MIT domain and another ubiquitin isopeptidase, AMSH, reveals common interactions with CHMP1A and CHMP1B but a distinct selectivity of AMSH for CHMP3/VPS24, a core subunit of the ESCRT-III complex, and UBPY for CHMP7.
Molecular genetics of bipolar disorder and depression.
Kato, Wako, Japan. In Psychiatry Clin Neurosci, 2007
GPR50 (Xq28), Citron (12q24), CHMP1.5 (18p11.2),
Structure and ESCRT-III protein interactions of the MIT domain of human VPS4A.
Sundquist et al., Salt Lake City, United States. In Proc Natl Acad Sci U S A, 2005
CHMP1B is bound by the VPS4A microtubule interacting and transport (MIT) domain.
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