Presentation Title

Regulation of the AMPK and mTORC1 Pathways by AK4 Expression to Promote Cell Proliferation

Faculty Mentor

Dr. Nathan Lanning

Start Date

18-11-2017 12:30 PM

End Date

18-11-2017 1:30 PM

Location

BSC-Ursa Minor 48

Session

Poster 2

Type of Presentation

Poster

Subject Area

biological_agricultural_sciences

Abstract

Adenylate kinase 4, a nuclear-encoded, mitochondrial protein, has been shown to play a role regulating cellular bioenergetics when gene expression is reduced by siRNA knockdown. Preliminary data suggests that the absence of AK4 in the mitochondria increases cellular ATP levels and causes aberrant signal transduction. Suppressed AK4 activates mammalian target of rampamycin complex 1 (mTORC 1) and AMP-activated protein kinase (AMPK) pathways, two important energy-sensitive regulators of homeostasis and proliferation. AMPK activation leads to downstream effector phosphorylation and initiates catabolic pathways, generating increased cellular ATP while initiating cell stress-responses. AK4 knockdown’s influence on the AMPK signaling pathway results in an increased phosphorylation of AMPK at T172, a biomarker of catabolic investment. Initiation of stress responses is observed by enhanced autophagy and cell survival under metabolic stress. Activation of these effects of AMPK signaling along with other mTORC1-sepcific effects can provide a mechanism by which cancer cells can thrive, thus highlighting the importance of examining the mechanism by which AK4 exerts its influence both mTORC 1 and AMPK signaling. CSU-LSAMP is supported by, National Science Foundation under Grant # HRD-1302873 and the CSU Office of the Chancellor. Additional funding was from the National Institutes of Health Grant # R15GM123382.

Summary of research results to be presented

AK4 expression regulates the activation of AMPK and mTORC1 pathways, resulting in increased cellular ATP levels and elevated cell-stress responses.

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Nov 18th, 12:30 PM Nov 18th, 1:30 PM

Regulation of the AMPK and mTORC1 Pathways by AK4 Expression to Promote Cell Proliferation

BSC-Ursa Minor 48

Adenylate kinase 4, a nuclear-encoded, mitochondrial protein, has been shown to play a role regulating cellular bioenergetics when gene expression is reduced by siRNA knockdown. Preliminary data suggests that the absence of AK4 in the mitochondria increases cellular ATP levels and causes aberrant signal transduction. Suppressed AK4 activates mammalian target of rampamycin complex 1 (mTORC 1) and AMP-activated protein kinase (AMPK) pathways, two important energy-sensitive regulators of homeostasis and proliferation. AMPK activation leads to downstream effector phosphorylation and initiates catabolic pathways, generating increased cellular ATP while initiating cell stress-responses. AK4 knockdown’s influence on the AMPK signaling pathway results in an increased phosphorylation of AMPK at T172, a biomarker of catabolic investment. Initiation of stress responses is observed by enhanced autophagy and cell survival under metabolic stress. Activation of these effects of AMPK signaling along with other mTORC1-sepcific effects can provide a mechanism by which cancer cells can thrive, thus highlighting the importance of examining the mechanism by which AK4 exerts its influence both mTORC 1 and AMPK signaling. CSU-LSAMP is supported by, National Science Foundation under Grant # HRD-1302873 and the CSU Office of the Chancellor. Additional funding was from the National Institutes of Health Grant # R15GM123382.