Binds to the plus end of microtubules and regulates the dynamics of the microtubule cytoskeleton. Promotes microtubule growth and microtubule bundling. Links cytoplasmic vesicles to microtubules and thereby plays an important role in intracellular vesicle trafficking. Plays a role macropinocytosis and endosome trafficking. (updated: Oct. 10, 2018)
The data and differentiation stages presented below come from the proteomic study and analysis performed by our partners of the GReX consortium, more details are available in their published work.
No sequence conservation computed yet.
Total structural coverage: 0%
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The reference OMIM entry for this protein is 179838
Cap-gly domain-containing linker protein 1; clip1
Restin; rsn
Reed-sternberg microtubule-associated protein
Cytoplasmic linker 1; cyln1
Cytoplasmic linker protein 170; clip170
DESCRIPTION
CLIP1 encodes a member of the microtubule (MT) plus-end tracking protein family. It has an important role in spermatogenesis as well as in neuronal development (summary by Larti et al., 2015).
CLONING
Binding of endocytic carrier vesicles to microtubules depends on the microtubule-binding protein CLIP170 in vitro. In vivo, CLIP170 colocalizes with a subset of transferrin receptor-positive endocytic structures and, more extensively, with endosomal tubules induced by brefeldin A. Pierre et al. (1992) cloned a cDNA for CLIP70 and found that the predicted protein contains 1,392 amino acids. The predicted nonhelical C- and N-terminal domains of the homodimeric protein are connected by a long coiled-coil domain. Pierre et al. (1992) identified a novel motif present in a tandem repeat in the N-terminal domain of CLIP170 that is involved in binding to microtubules. This motif is also found in the Drosophila Glued and yeast BIK1 proteins. These features, together with its very elongated structure, suggested that CLIP170 belongs to a novel class of proteins, designated cytoplasmic linker proteins (CLIPs), that mediate interactions of organelles with microtubules. Restin, initially thought to be an intermediate filament-associated protein, is in fact associated with microtubules, as shown by immunofluorescence microscopy (Pierre et al., 1994). Its expression is limited to Reed-Sternberg cells, characteristic of Hodgkin disease, and in vitro cultivated peripheral blood monocytes (Bilbe et al., 1992; Delabie et al., 1992). The protein was named restin by Bilbe et al. (1992) because of its specific expression in the Reed-Sternberg cell. Bilbe et al. (1992) suggested that its overexpression may be a contributing factor in the progression of Hodgkin disease. Delabie et al. (1992) found that restin was not detectable in normal tissues, a range of B- and T-cell non-Hodgkin lymphomas, and nonlymphoid tumors. Restin was present in Reed-Sternberg cells and variants thereof in Hodgkin disease, with the exception of the lymphocyte-predominant, paragranuloma subtype. Irsch et al. (1998) described the isolation of viable mononucleated Hodgkin and Reed-Sternberg and bi- or oligonucleated Reed-Sternberg cells from Hodgkin disease tissues. CLIP170 and restin are identical except for a 35-amino acid insert in restin that is absent in CLIP170. Griparic and Keller (1998) identified 2 variants of CLIP170: CLIP170(11), which contains an 11-amino acid insert instead of the 35-amino acid restin insert, and CLIP170(11+35), which contains both the 11-amino acid insert and the 35-amino acid restin insert. Both novel isoforms were found to be preferentially expressed in muscle tissue.
GENE FUNCTION
Perez et al. (1999) found that CLIP170 binds in stretches along a subset of microtubule ends. These stretches appeared to move with the growing tips of microtubules at 0.15 to 0.4 micro m/s, comparable to microtubule elongation in vivo. Analysis of speckles along dynamic CLIP170 stretches suggested that CLIP170 treadmills on growing microtubule ends rather than being continuously transported toward these ends. Drugs affecting microtubule dynamics rapidly inhibited movement of CLIP170 dashes. Perez et al. (1999) proposed that CLIP170 highlights growing microtubule ends by specifically recognizing the structure of a segment of newly polymerized tubulin. Fukata et al. (2002) found that IQGAP1 (
603379), an effector of RAC1 (
602048) and CDC4 ...
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Subscribe to this protein entry history
Dec. 10, 2018: Protein entry updated
Automatic update: model status changed
Nov. 17, 2018: Protein entry updated
Automatic update: OMIM entry 179838 was added.
Oct. 19, 2018: Additional information
Initial protein addition to the database. This entry was referenced in Bryk and co-workers. (2017).