PKD1 Inhibits AMPK2 through Phosphorylation of Serine 491 and Impairs Insulin Signaling in Skeletal Muscle Cells

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2016_ValentineR_PKD1_Inhibits_AMPK2_through_Phosphorylation.pdf (2.53 MB)
Date
2016-03-11
Authors
Coughlan, Kimberly
Valentine, Rudy
Sudit, Bella
Allen, Katherine
Dagon, Yossi
Kahn, Barbara
Ruderman, Neil
Saha, Asish
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Valentine, Rudy
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Kinesiology
The Department of Kinesiology seeks to provide an ample knowledge of physical activity and active living to students both within and outside of the program; by providing knowledge of the role of movement and physical activity throughout the lifespan, it seeks to improve the lives of all members of the community. Its options for students enrolled in the department include: Athletic Training; Community and Public Health; Exercise Sciences; Pre-Health Professions; and Physical Education Teacher Licensure. The Department of Physical Education was founded in 1974 from the merger of the Department of Physical Education for Men and the Department of Physical Education for Women. In 1981 its name changed to the Department of Physical Education and Leisure Studies. In 1993 its name changed to the Department of Health and Human Performance. In 2007 its name changed to the Department of Kinesiology. Dates of Existence: 1974-present. Historical Names: Department of Physical Education (1974-1981), Department of Physical Education and Leisure Studies (1981-1993), Department of Health and Human Performance (1993-2007). Related Units: College of Human Sciences (parent college), College of Education (parent college, 1974 - 2005), Department of Physical Education for Women (predecessor) Department of Physical Education for Men
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Abstract

Background: Diminished activity of the enzyme AMP-activated protein kinase (AMPK) is associated with impaired insulin signaling.

Results: Protein Kinase (PK)C/D1 activation inhibits AMPK2 via Ser491 phosphorylation; PKD1 inhibition prevents this in skeletal muscle cells.

Conclusion: PKD1 is a novel upstream AMPK-kinase that phosphorylates AMPK on Ser491 and regulates insulin signaling.

Significance: PKD1 inhibition may be a novel strategy for improving insulin sensitivity.
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This article is published as Coughlan KA, Valentine RJ, Sudit BS, Allen K, Dagon Y, Kahn BB, Ruderman NB, Saha AK. PKD1 inhibits AMPKα2 through phosphorylation of Ser491 and impairs insulin signaling in skeletal muscle cells. Journal Biological Chemistry. 2016; 291(11):5664-75. DOI: 10.1074/jbc.M115.696849. Posted with permission.
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http://doi.org/10.1074/jbc.M115.696849
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https://dr.lib.iastate.edu/handle/20.500.12876/52534
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Biomechanics
Endocrinology, Diabetes, and Metabolism
Exercise Science
Kinesiology
Motor Control
Psychology of Movement
Keywords
AMP-activated kinase (AMPK), Akt PKB, Serine485/491, insulin resistance, protein kinase C (PKC), protein kinase D (PKD), skeletal muscle
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Fri Jan 01 00:00:00 UTC 2016
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