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dc.contributor.author
Lee, C. Y.
dc.contributor.author
Bisig, Carlos Gaston
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Conrad, M. N.
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Ditamo, Yanina
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Almeida, L. Previato de
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Dresser, M.E.
dc.contributor.author
Pezza, Roberto
dc.date.available
2021-10-16T00:34:49Z
dc.date.issued
2020-01
dc.identifier.citation
Lee, C. Y.; Bisig, Carlos Gaston; Conrad, M. N.; Ditamo, Yanina; Almeida, L. Previato de; et al.; Telomere-led meiotic chromosome movements: recent update in structure and function; Taylor & Francis; Nucleus; 11; 9; 1-2020; 111-116
dc.identifier.issn
1949-1034
dc.identifier.uri
http://hdl.handle.net/11336/143967
dc.description.abstract
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.
dc.format
application/pdf
dc.language.iso
por
dc.publisher
Taylor & Francis
dc.rights
info:eu-repo/semantics/openAccess
dc.rights.uri
https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
dc.subject
CSM4
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LINC
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MPS2
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MYO2
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RAPID PROPHASE MOVEMENTS (RPMS)
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Bioquímica y Biología Molecular
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Ciencias Biológicas
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CIENCIAS NATURALES Y EXACTAS
dc.title
Telomere-led meiotic chromosome movements: recent update in structure and function
dc.type
info:eu-repo/semantics/article
dc.type
info:ar-repo/semantics/artículo
dc.type
info:eu-repo/semantics/publishedVersion
dc.date.updated
2021-09-06T15:07:25Z
dc.identifier.eissn
1949-1042
dc.journal.volume
11
dc.journal.number
9
dc.journal.pagination
111-116
dc.journal.pais
Reino Unido
dc.journal.ciudad
Londres
dc.description.fil
Fil: Lee, C. Y.. Oklahoma Medical Research Foundation; Estados Unidos
dc.description.fil
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
dc.description.fil
Fil: Conrad, M. N.. Oklahoma Medical Research Foundation; Estados Unidos
dc.description.fil
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
dc.description.fil
Fil: Almeida, L. Previato de. Oklahoma Medical Research Foundation; Estados Unidos
dc.description.fil
Fil: Dresser, M.E.. Oklahoma Medical Research Foundation; Estados Unidos
dc.description.fil
Fil: Pezza, Roberto. Oklahoma Medical Research Foundation; Estados Unidos
dc.journal.title
Nucleus
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/https://www.tandfonline.com/doi/full/10.1080/19491034.2020.1769456
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7781623/
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/https://doi.org/10.1080/19491034.2020.1769456
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