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• W2013970896 startingPage "e0124816" @default.
• W2013970896 abstract "The Par1 kinases, also known as microtubule affinity-regulating kinases (MARKs), are important for the establishment of cell polarity from worms to mammals. Dysregulation of these kinases has been implicated in autism, Alzheimer’s disease and cancer. Despite their important function in health and disease, it has been unclear how the activity of MARK/Par1 is regulated by signals from cell surface receptors. Here we show that MARK/Par1 is activated downstream of NMDA receptors in primary hippocampal neurons. Further, we show that this activation is dependent on protein kinase A (PKA), through the phosphorylation of Ser431 of Par4/LKB1, the major upstream kinase of MARK/Par1. Together, our data reveal a novel mechanism by which MARK/Par1 is activated at the neuronal synapse." @default.
• W2013970896 created "2016-06-24" @default.
• W2013970896 creator A5033927933 @default.
• W2013970896 creator A5036259640 @default.
• W2013970896 date "2015-05-01" @default.
• W2013970896 modified "2023-09-26" @default.
• W2013970896 title "MARK/Par1 Kinase Is Activated Downstream of NMDA Receptors through a PKA-Dependent Mechanism" @default.
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• W2013970896 doi "https://doi.org/10.1371/journal.pone.0124816" @default.
• W2013970896 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/4416788" @default.
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• W2013970896 hasPublicationYear "2015" @default.
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