CLIP-170 Highlights Growing Microtubule Ends In Vivo

Perez, Franck; Diamantopoulos, Georgios S.; Stalder, Romaine; Kreis, Thomas E.

doi:10.1016/s0092-8674(00)80656-x

Cited by 367 publications

(340 citation statements)

References 59 publications

Supporting

Mentioning

311

Contrasting

Unclassified

Order By: Relevance

“…In interphase, GFP-CLIP-170 moved through the cell in cometlike structures at plus ends of growing microtubules (data not shown), consistent with previous observations (Perez et al, 1999). However, we were unable to detect these comet-like structures in mitotic cells transfected with GFP-CLIP-170.…”

Section: Clip-170 Localizes To Microtubule Plus Ends During Mitosissupporting

confidence: 92%

See 1 more Smart Citation

CLIP-170 facilitates the formation of kinetochore–microtubule attachments

Tanenbaum

Galjart

Vugt³

et al. 2005

EMBO J

View full text Add to dashboard Cite

CLIP-170 is a microtubule 'plus end tracking' protein involved in several microtubule-dependent processes in interphase. At the onset of mitosis, CLIP-170 localizes to kinetochores, but at metaphase, it is no longer detectable at kinetochores. Although RNA interference (RNAi) experiments have suggested an essential role for CLIP-170 during mitosis, the molecular function of CLIP-170 in mitosis has not yet been revealed. Here, we used a combination of high-resolution microscopy and RNAi-mediated depletion to study the function of CLIP-170 in mitosis. We found that CLIP-170 dynamically localizes to the outer most part of unattached kinetochores and to the ends of growing microtubules. In addition, we provide evidence that a pool of CLIP-170 is transported along kinetochoremicrotubules by the dynein/dynactin complex. Interference with CLIP-170 expression results in defective chromosome congression and diminished kinetochoremicrotubule attachments, but does not detectibly affect microtubule dynamics or kinetochore-microtubule stability. Taken together, our results indicate that CLIP-170 facilitates the formation of kinetochore-microtubule attachments, possibly through direct capture of microtubules at the kinetochore.

show abstract

Section: Clip-170 Localizes To Microtubule Plus Ends During Mitosissupporting

confidence: 92%

“…CLIP-170 is the founding member of the þ TIPs (Perez et al, 1999). It has an N-terminal microtubule-binding domain, a long central coiled-coil domain, required for homodimerization, and a C-terminus with two zinc-finger domains.…”

Section: Introductionmentioning

confidence: 99%

CLIP-170 facilitates the formation of kinetochore–microtubule attachments

Tanenbaum

Galjart

Vugt³

et al. 2005

EMBO J

View full text Add to dashboard Cite

show abstract

“…CLIP-170 has been proposed to serve the initial docking role, because this protein can interact with both endosomes (Pierre et al, 1992) and the distal ends of microtubules (Rickard and Kreis, 1990). Short arrays of CLIP-170 treadmill at microtubule plus ends as they grow toward the periphery (Perez et al, 1999), providing a potential mechanism for attachment of peripheral endosomes and other structures (Dujardin et al, 1998).…”

Section: Association Of Dynactin and Clip-170 At Microtubule Endsmentioning

confidence: 99%

“…CLIP-170 contributes to the binding of endosomal membranes to microtubules in vitro (Pierre et al, 1992). In cells, CLIP-170 labels the growing ends of microtubules (Perez et al, 1999), an appropriate site for its proposed function. Microtubule binding is regulated by phosphorylation (Rickard and Kreis, 1991), providing a means for release of CLIP-170 (and associated cargo) from microtubules under circumstances in which a static interaction is no longer needed.…”

Section: Introductionmentioning

confidence: 99%

Role of Dynactin in Endocytic Traffic: Effects of Dynamitin Overexpression and Colocalization with CLIP-170

Valetti

Wetzel

Schrader

et al. 1999

MBoC

Self Cite

257

252

View full text Add to dashboard Cite

The flow of material from peripheral, early endosomes to late endosomes requires microtubules and is thought to be facilitated by the minus end-directed motor cytoplasmic dynein and its activator dynactin. The microtubule-binding protein CLIP-170 may also play a role by providing an early link to endosomes. Here, we show that perturbation of dynactin function in vivo affects endosome dynamics and trafficking. Endosome movement, which is normally bidirectional, is completely inhibited. Receptor-mediated uptake and recycling occur normally, but cells are less susceptible to infection by enveloped viruses that require delivery to late endosomes, and they show reduced accumulation of lysosomally targeted probes. Dynactin colocalizes at microtubule plus ends with CLIP-170 in a way that depends on CLIP-170’s putative cargo-binding domain. Overexpression studies using p150Glued, the microtubule-binding subunit of dynactin, and mutant and wild-type forms of CLIP-170 indicate that CLIP-170 recruits dynactin to microtubule ends. These data suggest a new model for the formation of motile complexes of endosomes and microtubules early in the endocytic pathway.

show abstract

“…GFP fusion proteins of each revealed that they track the plus-ends of growing microtubules in cells [4,5]. At the amino terminus of CLIP-170 are two tandem CAP-Gly microtubule binding domains [6].…”

Section: Introductionmentioning

confidence: 99%

Microtubule binding proteins CLIP‐170, EB1, and p150^Glued form distinct plus‐end complexes

et al. 2006

View full text Add to dashboard Cite

Microtubule plus-end proteins CLIP-170 and EB1 dynamically track the tips of growing microtubules in vivo. Here we examine the association of these proteins with microtubules in vitro. CLIP-170 binds tubulin dimers and co-assembles into growing microtubules. EB1 binds tubulin dimers more weakly, so no co-assembly is observed. However, EB1 binds to CLIP-170, and forms a co-complex with CLIP-170 and tubulin that is recruited to growing microtubule plus ends. The interaction between CLIP-170 and EB1 is competitively inhibited by the related CAP-Gly protein p150 Glued , which also localizes to microtubule plus ends in vivo. Based on these observations, we propose a model in which the formation of distinct plus-end complexes may differentially affect microtubule dynamics in vivo.

show abstract

CLIP-170 Highlights Growing Microtubule Ends In Vivo

Cited by 367 publications

References 59 publications

CLIP-170 facilitates the formation of kinetochore–microtubule attachments

CLIP-170 facilitates the formation of kinetochore–microtubule attachments

Role of Dynactin in Endocytic Traffic: Effects of Dynamitin Overexpression and Colocalization with CLIP-170

Microtubule binding proteins CLIP‐170, EB1, and p150^Glued form distinct plus‐end complexes

Contact Info

Product

Resources

About

CLIP-170 Highlights Growing Microtubule Ends In Vivo

Cited by 367 publications

References 59 publications

CLIP-170 facilitates the formation of kinetochore–microtubule attachments

CLIP-170 facilitates the formation of kinetochore–microtubule attachments

Role of Dynactin in Endocytic Traffic: Effects of Dynamitin Overexpression and Colocalization with CLIP-170

Microtubule binding proteins CLIP‐170, EB1, and p150Glued form distinct plus‐end complexes

Contact Info

Product

Resources

About

Microtubule binding proteins CLIP‐170, EB1, and p150^Glued form distinct plus‐end complexes