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http://hdl.handle.net/10261/40990
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Campo DC | Valor | Lengua/Idioma |
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dc.contributor.author | Andrés-Delgado, Laura | - |
dc.contributor.author | Antón, Olga M. | - |
dc.contributor.author | Madrid, Ricardo | - |
dc.contributor.author | Byrne, Jennifer A. | - |
dc.contributor.author | Alonso, Miguel A. | - |
dc.date.accessioned | 2011-10-11T16:43:52Z | - |
dc.date.available | 2011-10-11T16:43:52Z | - |
dc.date.issued | 2010-12-23 | - |
dc.identifier.citation | Blood 116:5919-5929 (2010) | es_ES |
dc.identifier.issn | 0006-4971 | - |
dc.identifier.uri | http://hdl.handle.net/10261/40990 | - |
dc.description | 7 Figures. The online version of this article contains a data supplement. | es_ES |
dc.description.abstract | Expression of the src-family kinase lymphocyte-specific protein tyrosine kinase (Lck) at the plasma membrane is essential for it to fulfill its pivotal role in signal transduction in T lymphocytes. MAL, an integral membrane protein expressed in specific types of lymphoma, has been shown to play an important role in targeting Lck to the plasma membrane. Here we report that MAL interacts with Inverted Formin2 (INF2), a formin with the atypical property of promoting not only actin polymerization but also its depolymerization. In Jurkat T cells, INF2 colocalizes with MAL at the cell periphery and pericentriolar endosomes and along microtubules. Videomicroscopic analysis revealed that the MAL+ vesicles transporting Lck to the plasma membrane move along microtubule tracks. Knockdown of INF2 greatly reduced the formation of MAL+ transport vesicles and the levels of Lck at the plasma membrane and impaired formation of a normal immunologic synapse. The actin polymerization and depolymerization activities of INF2 were both required for efficient Lck targeting. Cdc42 and Rac1, which bind to INF2, regulate Lck transport in both Jurkat and primary human T cells. Thus, INF2 collaborates with MAL in the formation of specific carriers for targeting Lck to the plasma membrane in a process regulated by Cdc42 and Rac1. | es_ES |
dc.description.sponsorship | We thank A. Jiménez and J. A. Rodríguez for technical assistance and Drs I. Correas, J. Millán, and F. Martín-Belmonte for their helpful comments. The expert technical advice of the personnel of the Optical and Confocal Microscopy and Flow CytCometry Units is gratefully acknowledged. This work was supported by grants (BFU2009-07886 and CONSOLIDER COAT CSD2009-00016) to M.A.A. from the Ministerio de Ciencia e Innovación (MICINN), Spain. | es_ES |
dc.language.iso | eng | es_ES |
dc.publisher | American Society of Hematology | es_ES |
dc.rights | closedAccess | es_ES |
dc.subject | kinase (Lck) | es_ES |
dc.subject | T lymphocytes | es_ES |
dc.title | Formin INF2 regulates MAL-mediated transport of Lck to the plasma membrane of human T lymphocytes | es_ES |
dc.type | artículo | es_ES |
dc.identifier.doi | 10.1182/blood-2010-08-300665 | - |
dc.description.peerreviewed | Peer reviewed | es_ES |
dc.relation.publisherversion | http://bloodjournal.hematologylibrary.org/content/116/26/5919.abstract | es_ES |
dc.identifier.e-issn | 1528-0020 | - |
dc.type.coar | http://purl.org/coar/resource_type/c_6501 | es_ES |
item.openairetype | artículo | - |
item.cerifentitytype | Publications | - |
item.languageiso639-1 | en | - |
item.grantfulltext | none | - |
item.openairecristype | http://purl.org/coar/resource_type/c_18cf | - |
item.fulltext | No Fulltext | - |
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