TY  - JOUR
A1  - Velnati, Suresh
A1  - Centonze, Sara
A1  - Girivetto, Federico
A1  - Capello, Daniela
A1  - Biondi, Ricardo M.
A1  - Bertoni, Alessandra
A1  - Cantello, Roberto
A1  - Ragnoli, Beatrice
A1  - Malerba, Mario
A1  - Graziani, Andrea
A1  - Baldanzi, Gianluca
T1  - Identification of key phospholipids that bind and activate atypical PKCs
T2  - Biomedicines
N2  - PKCζ and PKCι/λ form the atypical protein kinase C subgroup, characterised by a lack of regulation by calcium and the neutral lipid diacylglycerol. To better understand the regulation of these kinases, we systematically explored their interactions with various purified phospholipids using the lipid overlay assays, followed by kinase activity assays to evaluate the lipid effects on their enzymatic activity. We observed that both PKCζ and PKCι interact with phosphatidic acid and phosphatidylserine. Conversely, PKCι is unique in binding also to phosphatidylinositol-monophosphates (e.g., phosphatidylinositol 3-phosphate, 4-phosphate, and 5-phosphate). Moreover, we observed that phosphatidylinositol 4-phosphate specifically activates PKCι, while both isoforms are responsive to phosphatidic acid and phosphatidylserine. Overall, our results suggest that atypical Protein kinase C (PKC) localisation and activity are regulated by membrane lipids distinct from those involved in conventional PKCs and unveil a specific regulation of PKCι by phosphatidylinositol-monophosphates.
KW  - membrane
KW  - lipid-protein interaction
KW  - lipid signalling
KW  - kinase regulation
KW  - phosphatidylinositols
Y1  - 2021
UR  - http://publikationen.ub.uni-frankfurt.de/frontdoor/index/index/docId/56939
UR  - https://nbn-resolving.org/urn:nbn:de:hebis:30:3-569393
SN  - 2227-9059
VL  - 9
IS  - Article 45
PB  - MDPI
CY  - Basel
ER  -