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Arl8 and SKIP act together to link lysosomes to kinesin-1.

ABSTRACT: Lysosomes move bidirectionally on microtubules, and this motility can be stimulated by overexpression of the small GTPase Arl8. By using affinity chromatography, we find that Arl8-GTP binds to the soluble protein SKIP (SifA and kinesin-interacting protein, aka PLEKHM2). SKIP was originally identified as a target of the Salmonella effector protein SifA and found to bind the light chain of kinesin-1 to activate the motor on the bacteria's replicative vacuole. We show that in uninfected cells both Arl8 and SKIP are required for lysosomes to distribute away from the microtubule-organizing center. We identify two kinesin light chain binding motifs in SKIP that are required for lysosomes to accumulate kinesin-1 and redistribute to the cell periphery. Thus, Arl8 binding to SKIP provides a link from lysosomal membranes to plus-end-directed motility. A splice variant of SKIP that lacks a light chain binding motif does not stimulate movement, suggesting fine-tuning by alternative splicing.

SUBMITTER: Rosa-Ferreira C

PROVIDER: S-EPMC3240744 | biostudies-literature | 2011 Dec

REPOSITORIES: biostudies-literature

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Arl8 and SKIP act together to link lysosomes to kinesin-1.

Rosa-Ferreira Cláudia C Munro Sean S

Developmental cell 20111201 6

Lysosomes move bidirectionally on microtubules, and this motility can be stimulated by overexpression of the small GTPase Arl8. By using affinity chromatography, we find that Arl8-GTP binds to the soluble protein SKIP (SifA and kinesin-interacting protein, aka PLEKHM2). SKIP was originally identified as a target of the Salmonella effector protein SifA and found to bind the light chain of kinesin-1 to activate the motor on the bacteria's replicative vacuole. We show that in uninfected cells both ...[more]

PMID: 22172677

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Dataset Information

Arl8 and SKIP act together to link lysosomes to kinesin-1.

Publications

Arl8 and SKIP act together to link lysosomes to kinesin-1.

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