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PDBsum entry 3rdv
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Structural protein
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PDB id
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3rdv
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PDB id:
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| Name: |
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Structural protein
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Title:
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Structure of the slain2c-clipcg1 complex
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Structure:
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Cap-gly domain-containing linker protein 1. Chain: a, b, c, d. Fragment: cap-gly 1 domain, residues 56-127. Synonym: cytoplasmic linker protein 1, cytoplasmic linker protein 170 alpha-2, clip-170, reed-sternberg intermediate filament-associated protein, restin. Engineered: yes. Slain motif-containing protein 2. Chain: e, f, g, h.
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Source:
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Homo sapiens. Human. Organism_taxid: 9606. Gene: clip-170. Expressed in: escherichia coli. Expression_system_taxid: 562. Synthetic: yes. Other_details: polypeptide synthesis
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Resolution:
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1.75Å
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R-factor:
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0.184
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R-free:
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0.229
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Authors:
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C.Manatschal,V.Olieric,M.O.Steinmetz
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Key ref:
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B.van der Vaart
et al.
(2011).
SLAIN2 links microtubule plus end-tracking proteins and controls microtubule growth in interphase.
J Cell Biol,
193,
1083-1099.
PubMed id:
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Date:
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01-Apr-11
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Release date:
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29-Jun-11
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PROCHECK
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Headers
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References
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P30622
(CLIP1_HUMAN) -
CAP-Gly domain-containing linker protein 1 from Homo sapiens
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Seq:
Struc:
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1438 a.a.
70 a.a.
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Key: |
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PfamA domain |
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Secondary structure |
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CATH domain |
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J Cell Biol
193:1083-1099
(2011)
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PubMed id:
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SLAIN2 links microtubule plus end-tracking proteins and controls microtubule growth in interphase.
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B.van der Vaart,
C.Manatschal,
I.Grigoriev,
V.Olieric,
S.M.Gouveia,
S.Bjelic,
J.Demmers,
I.Vorobjev,
C.C.Hoogenraad,
M.O.Steinmetz,
A.Akhmanova.
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ABSTRACT
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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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Links
