Chromatin modifying protein 1A (Chmp1A) of the endosomal sorting complex required for transport (ESCRT)-III family activates ataxia telangiectasia mutated (ATM) for PanC-1 cell growth inhibition

Manohar, Sumanth; Harlow, Matt L.; Nguyen, H. V.; Li, Jing; Hankins, Gerald R.; Park, Maiyon

doi:10.4161/cc.10.15.15926

Cited by 19 publications

(25 citation statements)

References 53 publications

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“…The tumor suppressor protein p53 and its transcriptional target TSAP6 have been implicated in the regulation of exosome secretion (Yu et al, 2006), illustrating potential couplings between signaling and exosome biogenesis (Hupalowska and Miaczynska, 2012). Moreover, p53 activity has been linked to the ESCRT-III component Chmp1A (Manohar et al, 2011), further explaining a role for p53 in MVE and maybe exosome biogenesis.…”

Section: Biogenesis Of Evs and Cargo Selectionmentioning

confidence: 99%

Extracellular vesicles: Exosomes, microvesicles, and friends

Raposo

Stoorvogel

2013

Journal of Cell Biology

6,847

124

6,182

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Cells release into the extracellular environment diverse types of membrane vesicles of endosomal and plasma membrane origin called exosomes and microvesicles, respectively. These extracellular vesicles (EVs) represent an important mode of intercellular communication by serving as vehicles for transfer between cells of membrane and cytosolic proteins, lipids, and RNA. Deficiencies in our knowledge of the molecular mechanisms for EV formation and lack of methods to interfere with the packaging of cargo or with vesicle release, however, still hamper identification of their physiological relevance in vivo. In this review, we focus on the characterization of EVs and on currently proposed mechanisms for their formation, targeting, and function.

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Section: Biogenesis Of Evs and Cargo Selectionmentioning

confidence: 99%

Extracellular vesicles: Exosomes, microvesicles, and friends

Raposo

Stoorvogel

2013

Journal of Cell Biology

6,847

124

6,182

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“…Potentially relevant observations include: 1) The original description of the ESCRT-III protein CHMP1A reported that it localized to chromatin, and appeared to play a role in creating regions of nuclease-resistant, condensed chromatin and associated with the transcriptional repressor polycomb-like protein (Pcl) on condensed chromatin (Stauffer et al, 2001). 2) Both CHMP1A and CHMP1B contain nuclear localization signals (Manohar et al, 2011;Yang et al, 2004). 3) CHMP4B localizes to chromosome bridges and micronuclei, and coimmunoprecipitates with chromatin (Sagona et al, 2014).…”

Section: Introductionmentioning

confidence: 99%

The ESCRT-III proteins IST1 and CHMP1B assemble around nucleic acids

Talledge

McCullough

Wenzel

et al. 2018

Preprint

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ESCRT-III proteins can promote inside-out or outside-in membrane tubulation and fission.In addition, several observations suggest that ESCRT factors may also associate with nucleic acids during development, different stages of the cell cycle, and during retrotransposition of parasitic nucleic acids like LINE1 elements. Two ESCRT-III subunits, IST1 (aka CHMP8) and CHMP1B, can coassemble as an external protein coat around liposomes in vitro and around recycling endosomal tubules in living cells. Here we show that recombinant IST1 and CHMP1B can also copolymerize into double stranded filaments that surround nucleic acids. Electron cryo-microscopy reconstructions of nucleic acid-bound IST1-CHMP1B copolymers revealed that the polynucleotides track along a binding groove formed between filaments of the inner CHMP1B strand. The well-ordered structures also reveal that the C-terminal tails of CHMP1B subunits extrude through the outer IST1 layer to the tube exterior. As a result, the MIT domain binding motifs of both CHMP1B and IST1 are arrayed on the outer surface of the copolymer, where they could bind and recruit MIT domain-containing co-factors, such as the SPASTIN ATPase or the USP8 ubiquitin protease. Our structure raises the possibility that ESCRT-III proteins may form nucleic acid complexes in mammalian cells.

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“…In addition, some phenotypes may result from loss of the nuclear function of Chmp1. For example, studies show that Chmp1 regulates the activity of Ataxia Telangiectasia Mutated (ATM) (Manohar et al, ) and p53 (Li et al, ), as well as the expression of BMI1/INK4 (Mochida et al, ) in mammalian cells through its nuclear function.…”

Section: Introductionmentioning

confidence: 99%

The drosophila Chmp1 protein determines wing cell fate through regulation of epidermal growth factor receptor signaling

Valentine

Hogan

Collier

2014

Developmental Dynamics

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BACKGROUND: Receptor down-regulation by the multivesicular body (MVB) pathway is critical for many cellular signaling events. MVB generation is mediated by the highly conserved ESCRT (0, I, II, and III) protein complexes. Chmp1 is an ESCRT-III component and a putative tumor suppressor in humans. However, published data on Chmp1 activity are conflicting and its role during tissue development is not well defined. RESULTS: We investigated the function of Drosophila Chmp1 and found that it is an essential gene. In the wing, loss of Chmp1 activity causes a cell fate change from intervein to vein, and interactions between Chmp1 and Drosophila Epidermal Growth Factor Receptor (DER) regulators suggest that Chmp1 negatively regulates DER signaling. Chmp1 knockdown also decreases Blistered expression, which is repressed by DER signaling. We find that Chmp1 protein localizes to the late endosome in Drosophila embryos, which is consistent with its effects on DER signaling resulting from its function in the ESCRT-III complex. CONCLUSIONS: Drosophila Chmp1 negatively regulates DER signaling, likely through its role in MVB formation. Loss of Chmp1 activity in the Drosophila wing induces a cell fate change from intervein to vein that should provide a useful tool for future studies of ESCRT protein activity. Developmental Dynamics 243:977-987, 2014. V C 2014 Wiley Periodicals, Inc.

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Chromatin modifying protein 1A (Chmp1A) of the endosomal sorting complex required for transport (ESCRT)-III family activates ataxia telangiectasia mutated (ATM) for PanC-1 cell growth inhibition

Cited by 19 publications

References 53 publications

Extracellular vesicles: Exosomes, microvesicles, and friends

Extracellular vesicles: Exosomes, microvesicles, and friends

The ESCRT-III proteins IST1 and CHMP1B assemble around nucleic acids

The drosophila Chmp1 protein determines wing cell fate through regulation of epidermal growth factor receptor signaling

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