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Gene Review:

Clip1 - CAP-GLY domain containing linker protein 1

Mus musculus

Synonyms: 1110007I12Rik, 4631429H07Rik, AV017631, C81039, CAP-Gly domain-containing linker protein 1, ...

Akhmanova, A. et al., Lansbergen, G. et al., Sikora-Polaczek, M. et al., Hoogenraad, C.C. et al., Kodama, A. et al., et al.

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High impact information on Clip1

In ACF7's absence, microtubules still bind EB1 and CLIP170, but they no longer grow along polarized actin bundles, nor do they pause and tether to actin-rich cortical sites [1].
Bleaching studies show that, as spermatogenesis progresses, GFP-CLIP-170 converts from a mobile plus-end-tracking protein to a relatively immobile protein [2].
We propose that CLIP-170 has a structural function in the male germline, in particular in spermatid differentiation and sperm head shaping [2].
We detect plus-end-tracking GFP-CLIP-170 in spermatogonia [2].
CLIP-170 is a microtubule "plus-end-tracking protein" implicated in the control of microtubule dynamics, dynactin localization, and the linking of endosomes to microtubules [2].

Biological context of Clip1

The end of prometaphase is correlated with checkpoint inactivation and disappearance of MAD2L1 (MAD2) and RSN (CLIP-170) proteins from kinetochores [3].
As spermatogenesis proceeds, GFP-CLIP-170 expression increases and the fusion protein strongly marks syncytia of differentiated spermatogonia and early prophase spermatocytes [2].
Here, we show that down-regulation of CLIP-170 by RNA interference results in a strongly reduced accumulation of dynactin at the MT tips [4].

Anatomical context of Clip1

CLIP-170 and CLIP-115 are cytoplasmic linker proteins that associate specifically with the ends of growing microtubules and may act as anti-catastrophe factors [5].
Using the knock-in mice, we followed GFP-CLIP-170 expression and behavior in dissected, live testis tubules [2].
Subsequently GFP-CLIP-170 levels drop, but during spermiogenesis (post-meiotic development), GFP-CLIP-170 accumulates again and is present on spermatid manchettes and centrosomes [2].
These anomalies may involve a mislocalization of CLIP170, which we find lacking in neurite extensions and growth cones of TTL null neurons [6].
In contrast with CLIP-170, CLIPR-59 is not localized to microtubules at steady state but is associated with the trans-Golgi network and the plasma membrane [7].

Associations of Clip1 with chemical compounds

By using scanning force microscopy and fluorescence resonance energy transfer-based experiments we provide evidence for an intramolecular interaction between the NH(2) and COOH termini of CLIP-170 [4].

Other interactions of Clip1

In transfected COS-1 cells, CLIP-115 initially accumulates at the distal ends of microtubules and coincides with CLIP-170, indicating that both proteins mark growing microtubule ends [8].

References

ACF7: an essential integrator of microtubule dynamics. Kodama, A., Karakesisoglou, I., Wong, E., Vaezi, A., Fuchs, E. Cell (2003) [Pubmed]
The microtubule plus-end-tracking protein CLIP-170 associates with the spermatid manchette and is essential for spermatogenesis. Akhmanova, A., Mausset-Bonnefont, A.L., van Cappellen, W., Keijzer, N., Hoogenraad, C.C., Stepanova, T., Drabek, K., van der Wees, J., Mommaas, M., Onderwater, J., van der Meulen, H., Tanenbaum, M.E., Medema, R.H., Hoogerbrugge, J., Vreeburg, J., Uringa, E.J., Grootegoed, J.A., Grosveld, F., Galjart, N. Genes Dev. (2005) [Pubmed]
The first mitosis of the mouse embryo is prolonged by transitional metaphase arrest. Sikora-Polaczek, M., Hupalowska, A., Polanski, Z., Kubiak, J.Z., Ciemerych, M.A. Biol. Reprod. (2006) [Pubmed]
Conformational changes in CLIP-170 regulate its binding to microtubules and dynactin localization. Lansbergen, G., Komarova, Y., Modesti, M., Wyman, C., Hoogenraad, C.C., Goodson, H.V., Lemaitre, R.P., Drechsel, D.N., van Munster, E., Gadella, T.W., Grosveld, F., Galjart, N., Borisy, G.G., Akhmanova, A. J. Cell Biol. (2004) [Pubmed]
Clasps are CLIP-115 and -170 associating proteins involved in the regional regulation of microtubule dynamics in motile fibroblasts. Akhmanova, A., Hoogenraad, C.C., Drabek, K., Stepanova, T., Dortland, B., Verkerk, T., Vermeulen, W., Burgering, B.M., De Zeeuw, C.I., Grosveld, F., Galjart, N. Cell (2001) [Pubmed]
A vital role of tubulin-tyrosine-ligase for neuronal organization. Erck, C., Peris, L., Andrieux, A., Meissirel, C., Gruber, A.D., Vernet, M., Schweitzer, A., Saoudi, Y., Pointu, H., Bosc, C., Salin, P.A., Job, D., Wehland, J. Proc. Natl. Acad. Sci. U.S.A. (2005) [Pubmed]
CLIPR-59 is a lipid raft-associated protein containing a cytoskeleton-associated protein glycine-rich domain (CAP-Gly) that perturbs microtubule dynamics. Lallemand-Breitenbach, V., Quesnoit, M., Braun, V., El Marjou, A., Poüs, C., Goud, B., Perez, F. J. Biol. Chem. (2004) [Pubmed]
Functional analysis of CLIP-115 and its binding to microtubules. Hoogenraad, C.C., Akhmanova, A., Grosveld, F., De Zeeuw, C.I., Galjart, N. J. Cell. Sci. (2000) [Pubmed]

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CLIP1	Bos taurus
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clip1a	Danio rerio
CLIP1	Gallus gallus
CLIP1	Homo sapiens
CLIP1	Macaca mulatta
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clip1	Xenopus (Silurana) tropicalis

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