J Cell Biol 2011,
PMID: 21646404
van der Vaart, Babet; Manatschal, Cristina; Grigoriev, Ilya; Olieric, Vincent; Gouveia, Susana Montenegro; Bjelic, Sasa; Demmers, Jeroen; Vorobjev, Ivan; Hoogenraad, Casper C; Steinmetz, Michel O; Akhmanova, Anna
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.
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Text Mining Data
SLAIN2 ⊣ ch-TOG: "
During mitosis,
SLAIN2 became highly phosphorylated, and its interaction with EBs and
ch-TOG was
inhibited
"
Manually curated Databases
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Gene Ontology Complexes microtubule plus-end:
microtubule plus-end complex (KIF18B-SLAIN2-CLIP1-MAPRE3-MAPRE1-KIF2C-MAPRE2)
In total, 21 gene pairs are associated to this article in curated databases