Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)

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Gene Review:

CLIP3 - CAP-GLY domain containing linker protein 3

Homo sapiens

Synonyms: CAP-Gly domain-containing linker protein 3, CLIP-170-related 59 kDa protein, CLIPR-59, CLIPR59, Cytoplasmic linker protein 170-related 59 kDa protein, ...

Perez, F. et al., Lallemand-Breitenbach, V. et al.

Perez, Pernet-Gallay, Nizak, Goodson, Kreis, Goud,

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High impact information on CLIP3

Consistent with this observation, overexpression of CLIPR-59 does not affect the microtubule network [1].
CLIPR-59, a new trans-Golgi/TGN cytoplasmic linker protein belonging to the CLIP-170 family [1].
The MTB domain of CLIPR-59 is functional because it localizes to microtubules when expressed as a fragment in HeLa cells [1].
CLIPR-59 contains an acidic region followed by three ankyrin-like repeats and two CLIP-170-related MTB motifs [1].
We report here the characterization of CLIPR-59, a CLIP-170-related protein localized to the trans-most part of the Golgi apparatus [1].

Associations of CLIP3 with chemical compounds

In contrast with the CLIP-170 microtubule-binding domain, the CLIPR-59 microtubule-binding domain diminishes microtubule regrowth after nocodazole washout in vivo, showing that this domain can prevent microtubule polymerization [2].

References

CLIPR-59, a new trans-Golgi/TGN cytoplasmic linker protein belonging to the CLIP-170 family. Perez, F., Pernet-Gallay, K., Nizak, C., Goodson, H.V., Kreis, T.E., Goud, B. J. Cell Biol. (2002) [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]

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