Insulin Promotes Formation of Polymerized Microtubules by a Phosphatidylinositol 3-Kinase-Independent, Actin-Dependent Pathway in 3T3-L1 Adipocytes
Endocrinology, ISSN: 0013-7227, Vol: 144, Issue: 11, Page: 5030-5039
2003
- 25Citations
- 17Captures
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Example: if you select the 1-year option for an article published in 2019 and a metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019. If you select the 3-year option for the same article published in 2019 and the metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019, 2018 and 2017.
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Metrics Details
- Citations25
- Citation Indexes25
- 25
- CrossRef19
- Captures17
- Readers17
- 17
Article Description
Direct demonstrations implicating the microtubule cytoskeleton in insulin-mediated adipose/muscle-specific glucose transporter (GLUT4) translocation are beginning to emerge, and one role of the microtubule network appears to be the provision of a solid support for GLUT4 vesicle movement. In the current study we show that insulin treatment increases total polymerized α-tubulin in microtubules in a time- and dose-dependent manner that coincides with established insulin-mediated changes in GLUT4 translocation. Insulin stimulates the growth of microtubules through a pathway that requires tyrosine kinase activity, as indicated by inhibition of the effect after treatment with genistein. Insulin-mediated growth was not inhibited by treatment with the MAPK kinase (MEK) inhibitor, PD98059 or by wortmannin, indicating that the effect does not require activation of extracellular signal- regulated kinase 1/2 or phosphatidylinositide 3-kinase. Depolymerization of the actin cytoskeleton with latrunculin B abrogated the effect of insulin on microtubule polymerization, indicating that an intact actin network is a requirement for insulin-dependent modulation of microtubules. Using methods that measure insulin-dependent GLUT4 translocation in populations of adipocytes as opposed to individual cells, we show a statistically significant reduction in translocation (30% inhibition) in the presence of low concentrations of nocodazole (2 μM). This concentration incompletely depolymerizes the microtubule network, revealing that partial depolymerization of microtubules is sufficient to inhibit GLUT4 translocation. It is likely that stabilization of the microtubule network contributes to insulin stimulation of GLUT4 translocation.
Bibliographic Details
http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=0242552004&origin=inward; http://dx.doi.org/10.1210/en.2003-0609; http://www.ncbi.nlm.nih.gov/pubmed/12959978; https://academic.oup.com/endo/article/144/11/5030/2881008; https://dx.doi.org/10.1210/en.2003-0609; https://academic.oup.com/endo/article-abstract/144/11/5030/2881008?redirectedFrom=fulltext
The Endocrine Society
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