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J Cell Biol. 2011 Jun 13;193(6):1083-99. doi: 10.1083/jcb.201012179. Epub 2011 Jun 6.

SLAIN2 links microtubule plus end-tracking proteins and controls microtubule growth in interphase.

Author information

1
Department of Cell Biology, Erasmus Medical Center, 3000 CA Rotterdam, Netherlands.

Abstract

The ends of growing microtubules (MTs) accumulate a set of diverse factors known as MT plus end-tracking proteins (+TIPs), which control microtubule dynamics and organization. In this paper, we identify SLAIN2 as a key component of +TIP interaction networks. We showed that the C-terminal part of SLAIN2 bound to end-binding proteins (EBs), cytoplasmic linker proteins (CLIPs), and CLIP-associated proteins and characterized in detail the interaction of SLAIN2 with EB1 and CLIP-170. Furthermore, we found that the N-terminal part of SLAIN2 interacted with ch-TOG, the mammalian homologue of the MT polymerase XMAP215. Through its multiple interactions, SLAIN2 enhanced ch-TOG accumulation at MT plus ends and, as a consequence, strongly stimulated processive MT polymerization in interphase cells. Depletion or disruption of the SLAIN2-ch-TOG complex led to disorganization of the radial MT array. During mitosis, SLAIN2 became highly phosphorylated, and its interaction with EBs and ch-TOG was inhibited. Our study provides new insights into the molecular mechanisms underlying cell cycle-specific regulation of MT polymerization and the organization of the MT network.

PMID:
21646404
PMCID:
PMC3115796
DOI:
10.1083/jcb.201012179
[Indexed for MEDLINE]
Free PMC Article

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