SLAIN2 links microtubule plus end-tracking proteins and controls microtubule growth in interphase |
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Authors: | 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 |
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Institution: | Department of Cell Biology, Erasmus Medical Center, 3000 CA Rotterdam, Netherlands. |
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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. |
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