@inbook{a35f2e0afbbc4affb5b8444fa1fd4c24,
title = "Photoreceptor neuroprotection: Regulation of akt activation through serine/threonine phosphatases, PHLPP and PHLPPL",
abstract = "Serine/threonine kinase Akt is a downstream effector of insulin receptor/ PI3K pathway that is involved in many processes, including providing neuroprotection to stressed rod photoreceptor cells. Akt signaling is known to be regulated by the serine/threonine phosphatases, PHLPP (PH domain and leucine rich repeat protein phosphatase) and PHLPPL (PH domain and leucine rich repeat protein phosphatase-like). We previously reported that both phosphatases are expressed in the retina, as well as in photoreceptor cells. In this study, we examined the PHLPP and PHLPPL phosphatase activities towards non-physiological and physiological substrates. Our results suggest that PHLPP was more active than PHLPPL towards non-physiological substrates, whereas both PHLPP and PHLPP dephosphorylated the physiological substrates of Akt1 and Akt3 with similar efficiencies. Our results also suggest that knockdown of PHLPPL alone does not increase Akt phosphorylation, due to a compensatory increase of PHLPP, which results in the dephosphorylation of Akt. Therefore, PHLPP and PHLPPL regulate Akt activation together when both phosphatases are expressed.",
keywords = "Activation, Akt, Neuroprotection, PHLPP, PHLPPL, Phosphatases, Photoreceptors",
author = "Rajala, {Raju V.S.} and Yogita Kanan and Anderson, {Robert E.}",
note = "Publisher Copyright: {\textcopyright} Springer International Publishing Switzerland 2016.",
year = "2016",
month = oct,
day = "1",
doi = "10.1007/978-3-319-17121-0_55",
language = "English (US)",
series = "Advances in Experimental Medicine and Biology",
publisher = "Springer New York LLC",
pages = "419--424",
booktitle = "Advances in Experimental Medicine and Biology",
}