Unknown

Dataset Information

0

Minimal plus-end tracking unit of the cytoplasmic linker protein CLIP-170.


ABSTRACT: Cytoplasmic linker protein 170 (CLIP-170) is the prototype microtubule (MT) plus-end tracking protein (+TIP) and is involved in regulating MT dynamics. A comprehensive understanding of the process by which CLIP-170 tracks MT plus ends would provide insight into its function. However, the precise molecular mechanism of CLIP-170 +TIP behavior is unknown, and many potential models have been presented. Here, by separating the two CLIP-170 CAP-Gly domains and their adjacent serine-rich regions into fragments of varied size, we have characterized the minimal plus-end tracking unit of CLIP-170 in vivo. Each CLIP-170 fragment was also characterized for its tubulin polymerization activity in vitro. We found that the two CAP-Gly domains have different activities, whereas CAP-Gly-1 appears incompetent to mediate either +TIP behavior or MT nucleation, a CLIP-170 fragment consisting of the second CAP-Gly domain and its adjacent serine-rich region can both track MT plus ends in vivo and induce tubulin polymerization in vitro. These observations complement recent work on CLIP-170 fragments, demonstrate that CAP-Gly motifs do not require dimerization for +TIP and polymerization-promoting activities, and provide insight into CLIP-170 function and mechanism.

SUBMITTER: Gupta KK 

PROVIDER: S-EPMC2652304 | biostudies-literature | 2009 Mar

REPOSITORIES: biostudies-literature

altmetric image

Publications

Minimal plus-end tracking unit of the cytoplasmic linker protein CLIP-170.

Gupta Kamlesh K KK   Paulson Benjamin A BA   Folker Eric S ES   Charlebois Blake B   Hunt Alan J AJ   Goodson Holly V HV  

The Journal of biological chemistry 20081213 11


Cytoplasmic linker protein 170 (CLIP-170) is the prototype microtubule (MT) plus-end tracking protein (+TIP) and is involved in regulating MT dynamics. A comprehensive understanding of the process by which CLIP-170 tracks MT plus ends would provide insight into its function. However, the precise molecular mechanism of CLIP-170 +TIP behavior is unknown, and many potential models have been presented. Here, by separating the two CLIP-170 CAP-Gly domains and their adjacent serine-rich regions into f  ...[more]

Similar Datasets

| S-EPMC2626730 | biostudies-literature
| S-EPMC1266433 | biostudies-literature
| S-EPMC2052927 | biostudies-literature
| S-EPMC1257404 | biostudies-literature
| S-EPMC2174080 | biostudies-literature
| S-EPMC6341378 | biostudies-literature
| S-EPMC2912352 | biostudies-literature
| S-EPMC4395129 | biostudies-literature
| S-EPMC4621836 | biostudies-literature
| S-EPMC2883945 | biostudies-literature