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Regulation of mouse oocyte microtubule and organelle dynamics by PADI6 and the cytoplasmic lattices.


ABSTRACT: Organelle positioning and movement in oocytes is largely mediated by microtubules (MTs) and their associated motor proteins. While yet to be studied in germ cells, cargo trafficking in somatic cells is also facilitated by specific recognition of acetylated MTs by motor proteins. We have previously shown that oocyte-restricted PADI6 is essential for formation of a novel oocyte-restricted fibrous structure, the cytoplasmic lattices (CPLs). Here, we show that ?-tubulin appears to be associated with the PADI6/CPL complex. Next, we demonstrate that organelle positioning and redistribution is defective in PADI6-null oocytes and that alteration of MT polymerization or MT motor activity does not induce organelle redistribution in these oocytes. Finally, we report that levels of acetylated microtubules are dramatically suppressed in the cytoplasm of PADI6-null oocytes, suggesting that the observed organelle redistribution failure is due to defects in stable cytoplasmic MTs. These results demonstrate that the PADI6/CPL superstructure plays a key role in regulating MT-mediated organelle positioning and movement.

SUBMITTER: Kan R 

PROVIDER: S-EPMC3031771 | biostudies-literature | 2011 Feb

REPOSITORIES: biostudies-literature

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Regulation of mouse oocyte microtubule and organelle dynamics by PADI6 and the cytoplasmic lattices.

Kan Rui R   Yurttas Piraye P   Kim Boram B   Jin Mei M   Wo Luccie L   Lee Bora B   Gosden Roger R   Coonrod Scott A SA  

Developmental biology 20101211 2


Organelle positioning and movement in oocytes is largely mediated by microtubules (MTs) and their associated motor proteins. While yet to be studied in germ cells, cargo trafficking in somatic cells is also facilitated by specific recognition of acetylated MTs by motor proteins. We have previously shown that oocyte-restricted PADI6 is essential for formation of a novel oocyte-restricted fibrous structure, the cytoplasmic lattices (CPLs). Here, we show that α-tubulin appears to be associated with  ...[more]

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