Identification of an oncoprotein-and UV-responsive protein kinase that binds and potentiates the c-Jun activation domain.
M Hibi, A Lin, T Smeal, A Minden… - Genes & …, 1993 - genesdev.cshlp.org
The activity of c-Jun is regulated by phosphorylation. Various stimuli including transforming
oncogenes and UV light, induce phosphorylation of serines 63 and 73 in the amino-terminal …
oncogenes and UV light, induce phosphorylation of serines 63 and 73 in the amino-terminal …
JNK2 contains a specificity-determining region responsible for efficient c-Jun binding and phosphorylation.
T Kallunki, B Su, I Tsigelny, HK Sluss… - Genes & …, 1994 - genesdev.cshlp.org
The transcriptional activity of c-Jun is augmented through phosphorylation at two sites by a c-
Jun amino-terminal kinase (JNK). All cells express two distinct JNK activities, 46 and 55 kD …
Jun amino-terminal kinase (JNK). All cells express two distinct JNK activities, 46 and 55 kD …
c-Jun N-terminal phosphorylation correlates with activation of the JNK subgroup but not the ERK subgroup of mitogen-activated protein kinases
A Minden, A Lin, T Smeal, B Dérijard… - … and cellular biology, 1994 - Am Soc Microbiol
Abstract c-Jun transcriptional activity is stimulated by phosphorylation at two N-terminal
sites: Ser-63 and-73. Phosphorylation of these sites is enhanced in response to a variety of …
sites: Ser-63 and-73. Phosphorylation of these sites is enhanced in response to a variety of …
Activation of protein kinase C decreases phosphorylation of c-Jun at sites that negatively regulate its DNA-binding activity
WJ Boyle, T Smeal, LHK Defize, P Angel, JR Woodgett… - Cell, 1991 - cell.com
In resting human epithelial and fibroblastic cells, c-Jun is phosphorylated on serine and
threonine at five sites, three of which are phosphorylated in vitro by glycogen synthase …
threonine at five sites, three of which are phosphorylated in vitro by glycogen synthase …
Phorbol esters stimulate the phosphorylation of c-Jun but not v-Jun: regulation by the N-terminal delta domain.
V Adler, CC Franklin, AS Kraft - Proceedings of the National …, 1992 - National Acad Sciences
c-Jun and its oncogenic counterpart v-Jun are completely conserved within the region from
Ser-63 to Ser-73; these serines are sites for phorbol ester-inducible c-Jun phosphorylation …
Ser-63 to Ser-73; these serines are sites for phorbol ester-inducible c-Jun phosphorylation …
[HTML][HTML] Affinity-purified c-Jun amino-terminal protein kinase requires serine/threonine phosphorylation for activity.
V Adler, A Polotskaya, F Wagner, AS Kraft - Journal of Biological Chemistry, 1992 - Elsevier
The addition of phorbol esters to U937 leukemic cells stimulates the phosphorylation of c-
Jun on serines 63 and 73. To isolate the protein kinase which stimulates this …
Jun on serines 63 and 73. To isolate the protein kinase which stimulates this …
Intramolecular signal transduction in c‐Jun.
AG Papavassiliou, M Treier, D Bohmann - The EMBO journal, 1995 - embopress.org
The DNA‐binding activity of c‐Jun is determined by the phosphorylation state of a cluster of
threonine and serine residues located near its COOH‐terminus. We have analyzed the …
threonine and serine residues located near its COOH‐terminus. We have analyzed the …
Stress-activated protein kinases bind directly to the delta domain of c-Jun in resting cells: implications for repression of c-Jun function.
E Rubie, CC Franklin, A Kraft, DA Gillespie, J Avruch… - Oncogene, 1995 - europepmc.org
The transactivating function of the c-Jun proto-oncogene component of the AP-1
transcription factor is acutely regulated by a wide variety of cellular signals via modulation of …
transcription factor is acutely regulated by a wide variety of cellular signals via modulation of …
Oncoprotein-mediated signalling cascade stimulates c-Jun activity by phosphorylation of serines 63 and 73
T Smeal, B Binetruy, D Mercola… - … and Cellular Biology, 1992 - Taylor & Francis
In resting cells, c-Jun is phosphorylated on five sites. Three of these sites reside next to its
DNA binding domain and negatively regulate DNA binding. In response to expression of …
DNA binding domain and negatively regulate DNA binding. In response to expression of …
Altering the specificity of signal transduction cascades: positive regulation of c‐Jun transcriptional activity by protein kinase A.
Protein phosphorylation is commonly used to modulate transcription factor activity. However,
all existing genetic evidence for stimulation of transcription factor activity by phosphorylation …
all existing genetic evidence for stimulation of transcription factor activity by phosphorylation …