A conserved retromer-independent function for RAB-6.2 in C. elegans epidermis integrity.

Autor:	Kim JD; Department of Biology, Davidson College, Davidson, NC 28035, USA., Chun AY; Department of Biology, Davidson College, Davidson, NC 28035, USA., Mangan RJ; Department of Biology, Davidson College, Davidson, NC 28035, USA., Brown G; Department of Biology, Davidson College, Davidson, NC 28035, USA., Mourao Pacheco B; Department of Biology, Davidson College, Davidson, NC 28035, USA., Doyle H; Department of Biology, Davidson College, Davidson, NC 28035, USA., Leonard A; Department of Biology, Davidson College, Davidson, NC 28035, USA., El Bejjani R; Department of Biology, Davidson College, Davidson, NC 28035, USA raelbejjani@davidson.edu.
Jazyk:	angličtina
Zdroj:	Journal of cell science [J Cell Sci] 2019 Feb 15; Vol. 132 (5). Date of Electronic Publication: 2019 Feb 15.
DOI:	10.1242/jcs.223586
Abstrakt:	Rab proteins are conserved small GTPases that coordinate intracellular trafficking essential to cellular function and homeostasis. RAB-6.2 is a highly conserved C. elegans ortholog of human RAB6 proteins. RAB-6.2 is expressed in most tissues in C. elegans and is known to function in neurons and in the intestine to mediate retrograde trafficking. Here, we show that RAB-6.2 is necessary for cuticle integrity and impermeability in C. elegans RAB-6.2 functions in the epidermis to instruct skin integrity. Significantly, we show that expression of a mouse RAB6A cDNA can rescue defects in C. elegans epidermis caused by lack of RAB-6.2, suggesting functional conservation across phyla. We also show that the novel function of RAB-6.2 in C. elegans cuticle development is distinct from its previously described function in neurons. Exocyst mutants partially phenocopy rab-6.2 -null animals, and rab-6.2- null animals phenocopy mutants that have defective surface glycosylation. These results suggest that RAB-6.2 may mediate the trafficking of one or many secreted glycosylated cuticle proteins directly, or might act indirectly by trafficking glycosylation enzymes to their correct intracellular localization. Competing Interests: Competing interestsThe authors declare no competing or financial interests. (© 2019. Published by The Company of Biologists Ltd.)
Databáze:	MEDLINE
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