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

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

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Folker, Eric S. Gupta, Kamlesh K. Paulson, Benjamin A. Hunt, Alan J. Goodson, Holly V. Charlebois, Blake
Description	Author Affiliation: Gupta KK ( Department of Chemistry and Biochemistry, University of Notre Dame, Notre Dame, Indiana 46556, USA.)
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.
ISSN	00219258
e-ISSN	1083351X
Journal	Journal of Biological Chemistry
Issue Number	11
Volume Number	284
Language	English
Publisher	American Society for Biochemistry and Molecular Biology (United States)
Publisher Date	2009-03-13
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Microtubule-Associated Proteins Metabolism Microtubules Models, Biological Neoplasm Proteins Tubulin Amino Acid Motifs Physiology Animals COS Cells Cercopithecus Aethiops Genetics Protein Structure, Tertiary Swine Research Support, N.I.H., Extramural Biochemistry Molecular Biology
Content Type	Text
Resource Type	Article
Subject	Cell Biology Biochemistry Molecular Biology

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