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Dynein-mediated transport and membrane trafficking control PAR3 polarised distribution.

ABSTRACT: The scaffold protein PAR3 and the kinase PAR1 are essential proteins that control cell polarity. Their precise opposite localisations define plasma membrane domains with specific functions. PAR3 and PAR1 are mutually inhibited by direct or indirect phosphorylations, but their fates once phosphorylated are poorly known. Through precise spatiotemporal quantification of PAR3 localisation in the Drosophila oocyte, we identify several mechanisms responsible for its anterior cortex accumulation and its posterior exclusion. We show that PAR3 posterior plasma membrane exclusion depends on PAR1 and an endocytic mechanism relying on RAB5 and PI(4,5)P2. In a second phase, microtubules and the dynein motor, in connection with vesicular trafficking involving RAB11 and IKK-related kinase, IKK?, are required for PAR3 transport towards the anterior cortex. Altogether, our results point to a connection between membrane trafficking and dynein-mediated transport to sustain PAR3 asymmetry.

SUBMITTER: Jouette J

PROVIDER: S-EPMC6358217 | biostudies-literature | 2019 Jan

REPOSITORIES: biostudies-literature

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Dynein-mediated transport and membrane trafficking control PAR3 polarised distribution.

Jouette Julie J Guichet Antoine A Claret Sandra B SB

eLife 20190123

The scaffold protein PAR3 and the kinase PAR1 are essential proteins that control cell polarity. Their precise opposite localisations define plasma membrane domains with specific functions. PAR3 and PAR1 are mutually inhibited by direct or indirect phosphorylations, but their fates once phosphorylated are poorly known. Through precise spatiotemporal quantification of PAR3 localisation in the <i>Drosophila</i> oocyte, we identify several mechanisms responsible for its anterior cortex accumulation ...[more]

PMID: 30672465

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