3RDV

Structure of the SLAIN2c-CLIPCG1 complex

Summary for 3RDV

• Entry DOI: 10.2210/pdb3rdv/pdb
• Descriptor: CAP-Gly domain-containing linker protein 1, SLAIN motif-containing protein 2, SODIUM ION, ... (5 entities in total)
• Functional Keywords: cytoskeletal protein, cap gly protein complex, structural protein
• Biological source: Homo sapiens (human); More
• Cellular location: Cytoplasm : P30622; Cytoplasm, cytoskeleton: Q9P270
• Total number of polymer chains: 8
• Total formula weight: 36197.75

Authors

Manatschal, C.,Olieric, V.,Steinmetz, M.O. (deposition date: 2011-04-01, release date: 2011-06-29, Last modification date: 2023-11-01)

Primary citation

van der Vaart, B.,Manatschal, C.,Grigoriev, I.,Olieric, V.,Gouveia, S.M.,Bjelic, S.,Demmers, J.,Vorobjev, I.,Hoogenraad, C.C.,Steinmetz, M.O.,Akhmanova, A.
SLAIN2 links microtubule plus end-tracking proteins and controls microtubule growth in interphase
J.Cell Biol., 193:1083-1099, 2011

PubMed 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.

PubMed: 21646404
DOI: 10.1083/jcb.201012179

Experimental method

X-RAY DIFFRACTION (1.75 Å)