Data/hora: 11/06/2024 00:47:36

Provedor de dados: 	5	
País: 	France	
Título: 	PAK1 Regulates MEC-17 Acetyltransferase Activity and Microtubule Acetylation during Proplatelet Extension	
Autores: 	Van Dijk, Juliette; Bompard, Guillaume; Rabeharivelo, Gabriel; Cau, Julien; Delsert, Claude; Morin, Nathalie.	
Data: 	2020-10	
Ano: 	2020	
Palavras-chave: 	Microtubules; Acetylation; Megakaryocytes; Proplatelet; P21-activated kinase 1 PAK1; Acetyltransferase MEC-17.	
Resumo: 	Mature megakaryocytes extend long processes called proplatelets from which platelets are released in the blood stream. The Rho GTPases Cdc42 and Rac as well as their downstream target, p21-activated kinase 2 (PAK2), have been demonstrated to be important for platelet formation. Here we address the role, during platelet formation, of PAK1, another target of the Rho GTPases. PAK1 decorates the bundled microtubules (MTs) of megakaryocyte proplatelets. Using a validated cell model which recapitulates proplatelet formation, elongation and platelet release, we show that lack of PAK1 activity increases the number of proplatelets but restrains their elongation. Moreover, in the absence of PAK1 activity, cells have hyperacetylated MTs and lose their MT network integrity. Using inhibitors of the tubulin deacetylase HDAC6, we demonstrate that abnormally high levels of MT acetylation are not sufficient to increase the number of proplatelets but cause loss of MT integrity. Taken together with our previous demonstration that MT acetylation is required for proplatelet formation, our data reveal that MT acetylation levels need to be tightly regulated during proplatelet formation. We identify PAK1 as a direct regulator of the MT acetylation levels during this process as we found that PAK1 phosphorylates the MT acetyltransferase MEC-17 and inhibits its activity.	
Tipo: 	Text	
Idioma: 	Inglês	
Identificador: 	https://archimer.ifremer.fr/doc/00654/76594/77743.pdf

https://archimer.ifremer.fr/doc/00654/76594/77744.zip

DOI:10.3390/ijms21207531

https://archimer.ifremer.fr/doc/00654/76594/	
Editor: 	MDPI AG	
Formato: 	application/pdf	
Fonte: 	International Journal Of Molecular Sciences (1422-0067) (MDPI AG), 2020-10 , Vol. 21 , N. 20 , P. 7531 (17p.)	
Fonte: 	info:eu-repo/semantics/openAccess

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