| A single genetic locus controls both expression of DPEP1/CHMP1A and kidney disease development via ferroptosis. | A single genetic locus controls both expression of DPEP1/CHMP1A and kidney disease development via ferroptosis.
Guan Y, Liang X, Ma Z, Hu H, Liu H, Miao Z, Linkermann A, Hellwege JN, Voight BF, Susztak K., Free PMC Article | 09/4/2021 |
| Findings show CHMP1A loss impairs secretion of SHH on ART-EVs, providing molecular mechanistic insights into the role of ESCRT proteins and EVs in the brain. | The ESCRT-III Protein CHMP1A Mediates Secretion of Sonic Hedgehog on a Distinctive Subtype of Extracellular Vesicles.
Coulter ME, Dorobantu CM, Lodewijk GA, Delalande F, Cianferani S, Ganesh VS, Smith RS, Lim ET, Xu CS, Pang S, Wong ET, Lidov HGW, Calicchio ML, Yang E, Gonzalez DM, Schlaeger TM, Mochida GH, Hess H, Lee WA, Lehtinen MK, Kirchhausen T, Haussler D, Jacobs FMJ, Gaudin R, Walsh CA., Free PMC Article | 01/11/2020 |
| Letter: rs6860 polymorphism of the CHMP1A gene, is associated with fibromyalgia susceptibility in southern Spanish women. | The TT genotype of the rs6860 polymorphism of the charged multivesicular body protein 1A gene is associated with susceptibility to fibromyalgia in southern Spanish women.
Estévez-López F, Aparicio VA, Ruiz JR, Martínez-González LJ, Delgado-Fernández M, Álvarez-Cubero MJ. | 09/29/2018 |
| we identified Ser(179) and Ser(182) located in the C-terminal region of the CHMP1A as major phosphorylation sites that cause a mobility shift. | Identification of phosphorylation sites in the C-terminal region of charged multivesicular body protein 1A (CHMP1A).
Maemoto Y, Shibata H, Maki M. | 02/15/2014 |
| Study reports the discovery of a chimeric RNA between ZC3HAV1L and CHMP1A in human, located on chromosome 7 and 16, respectively. The fusion occurs at an exon-exon boundary, and was detected both computationally and experimentally from different cells or tissue types. | Detection of a common chimeric transcript between human chromosomes 7 and 16.
Fang W, Wei Y, Kang Y, Landweber LF., Free PMC Article | 04/27/2013 |
| Our results suggest that CHMP1A serves as a critical link between cytoplasmic signals and BMI1-mediated chromatin modifications that regulate proliferation of central nervous system progenitor cells. | CHMP1A encodes an essential regulator of BMI1-INK4A in cerebellar development.
Mochida GH, Ganesh VS, de Michelena MI, Dias H, Atabay KD, Kathrein KL, Huang HT, Hill RS, Felie JM, Rakiec D, Gleason D, Hill AD, Malik AN, Barry BJ, Partlow JN, Tan WH, Glader LJ, Barkovich AJ, Dobyns WB, Zon LI, Walsh CA., Free PMC Article | 04/6/2013 |
| our results demonstrate that Chmp1A functions as a tumor suppressor gene in renal cells | Chmp1A acts as a tumor suppressor gene that inhibits proliferation of renal cell carcinoma.
You Z, Xin Y, Liu Y, Sun J, Zhou G, Gao H, Xu P, Chen Y, Chen G, Zhang L, Gu L, Chen Z, Han B, Xuan Y. | 06/9/2012 |
| Chmp1A regulates tumor growth through ATM sugnaling and that neclear locaization of Chmp1A is reqired for the growth inhibition and ATM activation. | 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 S, Harlow M, Nguyen H, Li J, Hankins GR, Park M., Free PMC Article | 12/17/2011 |
| Both Vps4A and CHMP1A localized in the vicinity of viral cytoplasmic assembly compartments, sites of viral maturation that develop in Cytomegalovirus-infected cells. Thus, ESCRT machinery is involved in the final steps of HCMV replication. | Human cytomegalovirus exploits ESCRT machinery in the process of virion maturation.
Tandon R, AuCoin DP, Mocarski ES., Free PMC Article | 01/21/2010 |
| Chmp1A is a novel tumor suppressor, especially in pancreas and that Chmp1A regulates tumor growth potentially through p53 signaling pathway. | Chmp1A functions as a novel tumor suppressor gene in human embryonic kidney and ductal pancreatic tumor cells.
Li J, Belogortseva N, Porter D, Park M. | 01/21/2010 |
| 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. | The MIT domain of UBPY constitutes a CHMP binding and endosomal localization signal required for efficient epidermal growth factor receptor degradation.
Row PE, Liu H, Hayes S, Welchman R, Charalabous P, Hofmann K, Clague MJ, Sanderson CM, Urbé S. | 01/21/2010 |