A proteome-wide screen for mammalian SxIP motif-containing microtubule plus-end tracking proteins

Kai Jiang; Grischa Toedt; Susana Montenegro Gouveia; Norman E. Davey; Shasha Hua; Babet van der Vaart; Ilya Grigoriev; Jesper Larsen; Lotte Bang Pedersen; Karel Bezstarosti; Mariana Lince-Faria; Jeroen Demmers; Michel O. Steinmetz; Toby J. Gibson; Anna Akhmanova

doi:10.1016/j.cub.2012.07.047

A proteome-wide screen for mammalian SxIP motif-containing microtubule plus-end tracking proteins

Kai Jiang, Grischa Toedt, Susana Montenegro Gouveia, Norman E. Davey, Shasha Hua, Babet van der Vaart, Ilya Grigoriev, Jesper Larsen, Lotte Bang Pedersen, Karel Bezstarosti, Mariana Lince-Faria, Jeroen Demmers, Michel O. Steinmetz, Toby J. Gibson, Anna Akhmanova

Cellebiologi og Fysiologi

127 Citationer (Scopus)

Abstract

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.

Originalsprog	Engelsk
Tidsskrift	Current biology : CB
Vol/bind	22
Udgave nummer	19
Sider (fra-til)	1800-1807
Antal sider	8
ISSN	0960-9822
DOI	https://doi.org/10.1016/j.cub.2012.07.047
Status	Udgivet - 9 okt. 2012

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10.1016/j.cub.2012.07.047

http://www.sciencedirect.com/science/article/pii/S096098221200872X

Citationsformater

Jiang, K., Toedt, G., Gouveia, S. M., Davey, N. E., Hua, S., Vaart, B. V. D., Grigoriev, I., Larsen, J., Pedersen, L. B., Bezstarosti, K., Lince-Faria, M., Demmers, J., Steinmetz, M. O., Gibson, T. J., & Akhmanova, A. (2012). A proteome-wide screen for mammalian SxIP motif-containing microtubule plus-end tracking proteins. Current biology : CB, 22(19), 1800-1807. https://doi.org/10.1016/j.cub.2012.07.047

Jiang, K, Toedt, G, Gouveia, SM, Davey, NE, Hua, S, Vaart, BVD, Grigoriev, I, Larsen, J, Pedersen, LB, Bezstarosti, K, Lince-Faria, M, Demmers, J, Steinmetz, MO, Gibson, TJ & Akhmanova, A 2012, 'A proteome-wide screen for mammalian SxIP motif-containing microtubule plus-end tracking proteins', Current biology : CB, bind 22, nr. 19, s. 1800-1807. https://doi.org/10.1016/j.cub.2012.07.047

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abstract = "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.",

author = "Kai Jiang and Grischa Toedt and Gouveia, {Susana Montenegro} and Davey, {Norman E.} and Shasha Hua and Vaart, {Babet van der} and Ilya Grigoriev and Jesper Larsen and Pedersen, {Lotte Bang} and Karel Bezstarosti and Mariana Lince-Faria and Jeroen Demmers and Steinmetz, {Michel O.} and Gibson, {Toby J.} and Anna Akhmanova",

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AU - Jiang, Kai

AU - Toedt, Grischa

AU - Gouveia, Susana Montenegro

AU - Davey, Norman E.

AU - Hua, Shasha

AU - Vaart, Babet van der

AU - Grigoriev, Ilya

AU - Larsen, Jesper

AU - Pedersen, Lotte Bang

AU - Bezstarosti, Karel

AU - Lince-Faria, Mariana

AU - Demmers, Jeroen

AU - Steinmetz, Michel O.

AU - Gibson, Toby J.

AU - Akhmanova, Anna

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N2 - 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.

AB - 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.

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DO - 10.1016/j.cub.2012.07.047

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ER -

A proteome-wide screen for mammalian SxIP motif-containing microtubule plus-end tracking proteins

Abstract

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