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Rab10 GTPase regulates ER dynamics and morphology.

Abstract：

:We have identified Rab10 as an ER-specific Rab GTPase that regulates ER structure and dynamics. We show that Rab10 localizes to the ER and to dynamic ER-associated structures that track along microtubules and mark the position of new ER tubule growth. Rab10 depletion or expression of a Rab10 GDP-locked mutant alters ER morphology, resulting in fewer ER tubules. We demonstrate that this defect is due to a reduced ability of dynamic ER tubules to grow out and successfully fuse with adjacent ER. Consistent with this function, Rab10 partitions to dynamic ER-associated domains found at the leading edge of almost half of all dynamic ER tubules. Interestingly, this Rab10 domain is highly enriched with at least two ER enzymes that regulate phospholipid synthesis, phosphatidylinositol synthase (PIS) and CEPT1. Both the formation and function of this Rab10/PIS/CEPT1 dynamic domain are inhibited by expression of a GDP-locked Rab10 mutant. Together, these data demonstrate that Rab10 regulates ER dynamics and further suggest that these dynamics could be coupled to phospholipid synthesis.

journal_name

Nat Cell Biol

journal_title

Nature cell biology

authors

English AR,Voeltz GK

doi

10.1038/ncb2647

subject

Has Abstract

pub_date

2013-02-01 00:00:00

pages

169-78

issue

2

eissn

1465-7392

issn

1476-4679

pii

ncb2647

journal_volume

15

pub_type

杂志文章

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