FN Archimer Export Format
PT J
TI PAK1 Regulates MEC-17 Acetyltransferase Activity and Microtubule Acetylation during Proplatelet Extension
BT 
AF van Dijk, Juliette
   Bompard, Guillaume
   Rabeharivelo, Gabriel
   Cau, Julien
   Delsert, Claude
   Morin, Nathalie
AS 1:1,2;2:1,2;3:1,2;4:1,3,4;5:1,2,5;6:1,2;
FF 1:;2:;3:;4:;5:PDG-RBE-MARBEC-LAAAS;6:;
C1 Université de Montpellier, 34293 Montpellier, France
   CRBM, CNRS, UMR 5237, 1919 Route de Mende, 34293 Montpellier, France
   IGH, CNRS UMR 9002, 141, Rue de la Cardonille, 34396 Montpellier, France
   Montpellier Rio Imaging, 34293 Montpellier, France
   Station Expérimentale d’Aquaculture Ifremer, Chemin de Maguelone, 34250 Palavas-les-Flots, France
C2 UNIV MONTPELLIER, FRANCE
   CNRS, FRANCE
   CNRS, FRANCE
   MRI, FRANCE
   IFREMER, FRANCE
SI MONTPELLIER
SE PDG-RBE-MARBEC-LAAAS
IN WOS Ifremer UPR
   DOAJ
   copubli-france
   copubli-univ-france
IF 1.467
TC 6
UR https://archimer.ifremer.fr/doc/00654/76594/77743.pdf
   https://archimer.ifremer.fr/doc/00654/76594/77744.zip
LA English
DT Article
DE ;microtubules;acetylation;megakaryocytes;proplatelet;p21-activated kinase 1 PAK1;acetyltransferase MEC-17
AB 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. 
PY 2020
PD OCT
SO International Journal Of Molecular Sciences
SN 1422-0067
PU MDPI AG
VL 21
IS 20
UT 000585659000001
DI 10.3390/ijms21207531
ID 76594
ER

EF