FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W2297588052> ?p ?o ?g. }

• W2297588052 endingPage "20971" @default.
• W2297588052 startingPage "20960" @default.
• W2297588052 abstract "Protein kinases carry out important functions in cells both by phosphorylating substrates and by means of regulated non-catalytic activities. Such non-catalytic functions have been ascribed to many kinases, including some members of the Ste20 family. The Drosophila Ste20 kinase Slik phosphorylates and activates Moesin in developing epithelial tissues to promote epithelial tissue integrity. It also functions non-catalytically to promote epithelial cell proliferation and tissue growth. We carried out a structure-function analysis to determine how these two distinct activities of Slik are controlled. We find that the conserved C-terminal coiled-coil domain of Slik, which is necessary and sufficient for apical localization of the kinase in epithelial cells, is not required for Moesin phosphorylation but is critical for the growth-promoting function of Slik. Slik is auto- and trans-phosphorylated in vivo. Phosphorylation of at least two of three conserved sites in the activation segment is required for both efficient catalytic activity and non-catalytic signaling. Slik function is thus dependent upon proper localization of the kinase via the C-terminal coiled-coil domain and activation via activation segment phosphorylation, which enhances both phosphorylation of substrates like Moesin and engagement of effectors of its non-catalytic growth-promoting activity. Protein kinases carry out important functions in cells both by phosphorylating substrates and by means of regulated non-catalytic activities. Such non-catalytic functions have been ascribed to many kinases, including some members of the Ste20 family. The Drosophila Ste20 kinase Slik phosphorylates and activates Moesin in developing epithelial tissues to promote epithelial tissue integrity. It also functions non-catalytically to promote epithelial cell proliferation and tissue growth. We carried out a structure-function analysis to determine how these two distinct activities of Slik are controlled. We find that the conserved C-terminal coiled-coil domain of Slik, which is necessary and sufficient for apical localization of the kinase in epithelial cells, is not required for Moesin phosphorylation but is critical for the growth-promoting function of Slik. Slik is auto- and trans-phosphorylated in vivo. Phosphorylation of at least two of three conserved sites in the activation segment is required for both efficient catalytic activity and non-catalytic signaling. Slik function is thus dependent upon proper localization of the kinase via the C-terminal coiled-coil domain and activation via activation segment phosphorylation, which enhances both phosphorylation of substrates like Moesin and engagement of effectors of its non-catalytic growth-promoting activity." @default.
• W2297588052 created "2016-06-24" @default.
• W2297588052 creator A5004180056 @default.
• W2297588052 creator A5031854257 @default.
• W2297588052 creator A5049531033 @default.
• W2297588052 creator A5054954375 @default.
• W2297588052 creator A5061581101 @default.
• W2297588052 creator A5078181777 @default.
• W2297588052 creator A5089422969 @default.
• W2297588052 creator A5089670266 @default.
• W2297588052 date "2015-08-01" @default.
• W2297588052 modified "2023-10-11" @default.
• W2297588052 title "Regulation of Catalytic and Non-catalytic Functions of the Drosophila Ste20 Kinase Slik by Activation Segment Phosphorylation" @default.
• W2297588052 cites W1935419873 @default.
• W2297588052 cites W1963587413 @default.
• W2297588052 cites W1966704740 @default.
• W2297588052 cites W1968910405 @default.
• W2297588052 cites W1975016763 @default.
• W2297588052 cites W1978218402 @default.
• W2297588052 cites W1985279773 @default.
• W2297588052 cites W1987426979 @default.
• W2297588052 cites W1989461823 @default.
• W2297588052 cites W1993457391 @default.
• W2297588052 cites W1993926535 @default.
• W2297588052 cites W2001233441 @default.
• W2297588052 cites W2006733565 @default.
• W2297588052 cites W2015203780 @default.
• W2297588052 cites W2023331434 @default.
• W2297588052 cites W2033440293 @default.
• W2297588052 cites W2035121505 @default.
• W2297588052 cites W2036237432 @default.
• W2297588052 cites W2041120201 @default.
• W2297588052 cites W2041629876 @default.
• W2297588052 cites W2042015318 @default.
• W2297588052 cites W2042940417 @default.
• W2297588052 cites W2046093759 @default.
• W2297588052 cites W2047151879 @default.
• W2297588052 cites W2047669024 @default.
• W2297588052 cites W2048643631 @default.
• W2297588052 cites W2049065417 @default.
• W2297588052 cites W2050234810 @default.
• W2297588052 cites W2050771413 @default.
• W2297588052 cites W2052112605 @default.
• W2297588052 cites W2057212626 @default.
• W2297588052 cites W2058777736 @default.
• W2297588052 cites W2060020667 @default.
• W2297588052 cites W2061324224 @default.
• W2297588052 cites W2063716351 @default.
• W2297588052 cites W2065524217 @default.
• W2297588052 cites W2067677546 @default.
• W2297588052 cites W2070671255 @default.
• W2297588052 cites W2070879574 @default.
• W2297588052 cites W2073568903 @default.
• W2297588052 cites W2074883125 @default.
• W2297588052 cites W2075352286 @default.
• W2297588052 cites W2075725057 @default.
• W2297588052 cites W2080854317 @default.
• W2297588052 cites W2083106714 @default.
• W2297588052 cites W2083119850 @default.
• W2297588052 cites W2085250524 @default.
• W2297588052 cites W2091427349 @default.
• W2297588052 cites W2092128105 @default.
• W2297588052 cites W2115678668 @default.
• W2297588052 cites W2118460316 @default.
• W2297588052 cites W2118674189 @default.
• W2297588052 cites W2123117119 @default.
• W2297588052 cites W2123787611 @default.
• W2297588052 cites W2128674246 @default.
• W2297588052 cites W2130515511 @default.
• W2297588052 cites W2131459453 @default.
• W2297588052 cites W2135596918 @default.
• W2297588052 cites W2139362357 @default.
• W2297588052 cites W2149662085 @default.
• W2297588052 cites W2157658519 @default.
• W2297588052 cites W2162392252 @default.
• W2297588052 cites W2165160051 @default.
• W2297588052 cites W2165163773 @default.
• W2297588052 cites W2166542272 @default.
• W2297588052 cites W2171572099 @default.
• W2297588052 cites W2333046834 @default.
• W2297588052 cites W339644898 @default.
• W2297588052 doi "https://doi.org/10.1074/jbc.m115.645952" @default.
• W2297588052 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/4543655" @default.
• W2297588052 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/26170449" @default.
• W2297588052 hasPublicationYear "2015" @default.
• W2297588052 type Work @default.
• W2297588052 sameAs 2297588052 @default.
• W2297588052 citedByCount "11" @default.
• W2297588052 countsByYear W22975880522017 @default.
• W2297588052 countsByYear W22975880522018 @default.
• W2297588052 countsByYear W22975880522019 @default.
• W2297588052 countsByYear W22975880522020 @default.
• W2297588052 countsByYear W22975880522021 @default.
• W2297588052 countsByYear W22975880522022 @default.
• W2297588052 countsByYear W22975880522023 @default.
• W2297588052 crossrefType "journal-article" @default.
• W2297588052 hasAuthorship W2297588052A5004180056 @default.
• W2297588052 hasAuthorship W2297588052A5031854257 @default.

• next