Telomere-led meiotic chromosome movements: recent update in structure and function
Autor: | Yanina Ditamo, M. N. Conrad, Michael E. Dresser, L. Previato de Almeida, Chih-Ying Lee, Roberto J. Pezza, Carlos Gaston Bisig |
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Rok vydání: | 2020 |
Předmět: |
Models
Molecular Saccharomyces cerevisiae Proteins lcsh:QH426-470 RAPID PROPHASE MOVEMENTS (RPMS) LINC complex Saccharomyces cerevisiae macromolecular substances Biology Myo2 LINC MYO2 purl.org/becyt/ford/1 [https] 03 medical and health sciences Prophase Meiosis medicine lcsh:QH573-671 Nuclear membrane purl.org/becyt/ford/1.6 [https] Cytoskeleton Mps2 MPS2 030304 developmental biology 0303 health sciences lcsh:Cytology 030302 biochemistry & molecular biology Cell Biology Telomere Actin cytoskeleton Cell biology lcsh:Genetics Actin Cytoskeleton CSM4 Csm4 medicine.anatomical_structure Chromosome Structures Cytoplasm Commentary Chromosomes Fungal rapid prophase movements (RPMs) Article Commentary |
Zdroj: | CONICET Digital (CONICET) Consejo Nacional de Investigaciones Científicas y Técnicas instacron:CONICET Nucleus article-version (VoR) Version of Record Nucleus, Vol 11, Iss 1, Pp 111-116 (2020) |
ISSN: | 1949-1042 1949-1034 |
Popis: | In S. cerevisiae prophase meiotic chromosomes move by forces generated in the cytoplasm and transduced to the telomere via a protein complex located in the nuclear membrane. We know that chromosome movements require actin cytoskeleton [13,31] and the proteins Ndj1, Mps3, and Csm4. Until recently, the identity of the protein connecting Ndj1-Mps3 with the cytoskeleton components was missing. It was also not known the identity of a cytoplasmic motor responsible for interacting with the actin cytoskeleton and a protein at the outer nuclear envelope. Our recent work [36] identified Mps2 as the protein connecting Ndj1-Mps3 with cytoskeleton components; Myo2 as the cytoplasmic motor that interacts with Mps2; and Cms4 as a regulator of Mps2 and Myo2 interaction and activities (Figure 1). Below we present a model for how Mps2, Csm4, and Myo2 promote chromosome movements by providing the primary connections joining telomeres to the actin cytoskeleton through the LINC complex. Fil: Lee, C. Y.. Oklahoma Medical Research Foundation; Estados Unidos Fil: Bisig, Carlos Gaston. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Centro de Investigaciones en Química Biológica de Córdoba. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Centro de Investigaciones en Química Biológica de Córdoba; Argentina. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Departamento de Química Biológica; Argentina Fil: Conrad, M. N.. Oklahoma Medical Research Foundation; Estados Unidos Fil: Ditamo, Yanina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Centro de Investigaciones en Química Biológica de Córdoba. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Centro de Investigaciones en Química Biológica de Córdoba; Argentina. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Departamento de Química Biológica; Argentina Fil: Almeida, L. Previato de. Oklahoma Medical Research Foundation; Estados Unidos Fil: Dresser, M.E.. Oklahoma Medical Research Foundation; Estados Unidos Fil: Pezza, Roberto. Oklahoma Medical Research Foundation; Estados Unidos |
Databáze: | OpenAIRE |
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