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7150709 
Journal Article 
A Proteome-wide screen for mammalian SxIP motif-containing microtubule plus-end tracking proteins 
Jiang, K; Toedt, G; Montenegro Gouveia, S; Davey, NE; Hua, S; van Der Vaart, B; Grigoriev, I; Larsen, J; Pedersen, LB; Bezstarosti, K; Lince-Faria, M; Demmers, J; Steinmetz, MO; Gibson, TJ; Akhmanova, A; , 
2012 
Yes 
Current Biology
ISSN: 0960-9822
EISSN: 1879-0445 
English 
22885064 
Microtubule plus-end tracking proteins (+TIPs) are structurally and functionally diverse factors that accumulate at the growing microtubule plus-ends, connect them to various cellular structures, and control microtubule dynamics [1, 2]. EB1 and its homologs are +TIPs that can autonomously recognize growing microtubule ends and recruit to them a variety of other proteins. Numerous +TIPs bind to end binding (EB) proteins through natively unstructured basic and serine-rich polypeptide regions containing a core SxIP motif (serine-any amino acid-isoleucine-proline) [3]. The SxIP consensus sequence is short, and the surrounding sequences show high variability, raising the possibility that undiscovered SxIP containing +TIPs are encoded in mammalian genomes. Here, we performed a proteome-wide search for mammalian SxIP-containing +TIPs by combining biochemical and bioinformatics approaches. We have identified a set of previously uncharacterized EB partners that have the capacity to accumulate at the growing microtubule ends, including protein kinases, a small GTPase, centriole-, membrane-, and actin-associated proteins. We show that one of the newly identified +TIPs, CEP104, interacts with CP110 and CEP97 at the centriole and is required for ciliogenesis. Our study reveals the complexity of the mammalian +TIP interactome and provides a basis for investigating the molecular crosstalk between microtubule ends and other cellular structures.