Proteomics

Dataset Information

0

Mouse rod photoreceptor Prkaa1 knockout phosphoproteomics


ABSTRACT: Mouse rod photoreceptor specific Prkaa1 knockouts were isolated from retinas and processed for phosphoproteomics to elucidate downstream kinase targets. Prkaa1 is one of the isoforms for the catalytic subunit of AMP-activated protein kinase (AMPK), an essential nutrient sensing enzyme responsible for maintaining many metabolic processes.

INSTRUMENT(S): LTQ Orbitrap

ORGANISM(S): Mus Musculus (mouse)

TISSUE(S): Retinal Rod Cell, Retinal Rod

SUBMITTER: Tae Jun Lee  

LAB HEAD: Rajendra Apte

PROVIDER: PXD045667 | Pride | 2024-06-16

REPOSITORIES: Pride

Dataset's files

Source:
Action DRS
17171_ec04372_tc_903_P1_1.mzIdentML Mzid
17172_ec04373_tc_903_P1_2.mzIdentML Mzid
17173_ec04374_tc_903_P2.mzIdentML Mzid
ec04372_tc-903_P1_1.raw Raw
ec04373_tc-903_P1_2.raw Raw
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Publications

Catalytic isoforms of AMP-activated protein kinase differentially regulate IMPDH activity and photoreceptor neuron function.

Lee Tae Jun TJ   Sasaki Yo Y   Ruzycki Philip A PA   Ban Norimitsu N   Lin Joseph B JB   Wu Hung-Ting HT   Santeford Andrea A   Apte Rajendra S RS  

JCI insight 20240116 4


AMP-activated protein kinase (AMPK) plays a crucial role in maintaining ATP homeostasis in photoreceptor neurons. AMPK is a heterotrimeric protein consisting of α, β, and γ subunits. The independent functions of the 2 isoforms of the catalytic α subunit, PRKAA1 and PRKAA2, are uncharacterized in specialized neurons, such as photoreceptors. Here, we demonstrate in mice that rod photoreceptors lacking PRKAA2, but not PRKAA1, showed altered levels of cGMP, GTP, and ATP, suggesting isoform-specific  ...[more]

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