Regulation of the golgi apparatus by p38 and JNK kinases during cellular stress responses
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Regulation of the golgi apparatus by p38 and JNK kinases during cellular stress responses. / Nordgaard, Cathrine; Tollenaere, Maxim A.X.; Del Val, Ana Martinez; Bekker-Jensen, Dorte B.; Blasius, Melanie; Olsen, Jesper V.; Bekker-Jensen, Simon.
I: International Journal of Molecular Sciences, Bind 22, Nr. 17, 9595, 2021.Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt
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TY - JOUR
T1 - Regulation of the golgi apparatus by p38 and JNK kinases during cellular stress responses
AU - Nordgaard, Cathrine
AU - Tollenaere, Maxim A.X.
AU - Del Val, Ana Martinez
AU - Bekker-Jensen, Dorte B.
AU - Blasius, Melanie
AU - Olsen, Jesper V.
AU - Bekker-Jensen, Simon
N1 - Publisher Copyright: © 2021 by the authors. Licensee MDPI, Basel, Switzerland.
PY - 2021
Y1 - 2021
N2 - p38 and c-Jun N-terninal kinase (JNK) are activated in response to acute stress and inflammatory signals. Through modification of a plethora of substrates, these kinases profoundly re-shape cellular physiology for the optimal response to a harmful environment and/or an inflammatory state. Here, we utilized phospho-proteomics to identify several hundred substrates for both kinases. Our results indicate that the scale of signaling from p38 and JNK are of a similar magnitude. Among the many new targets, we highlight the regulation of the transcriptional regulators grb10-interacting GYF protein 1 and 2 (GIGYF1/2) by p38-dependent MAP kinase-activated protein kinase 2 (MK2) phosphorylation and 14–3–3 binding. We also show that the Golgi apparatus contains numerous substrates, and is a major target for regulation by p38 and JNK. When activated, these kinases mediate structural rearrangement of the Golgi apparatus, which positively affects protein flux through the secretory system. Our work expands on our knowledge about p38 and JNK signaling with important biological ramifications.
AB - p38 and c-Jun N-terninal kinase (JNK) are activated in response to acute stress and inflammatory signals. Through modification of a plethora of substrates, these kinases profoundly re-shape cellular physiology for the optimal response to a harmful environment and/or an inflammatory state. Here, we utilized phospho-proteomics to identify several hundred substrates for both kinases. Our results indicate that the scale of signaling from p38 and JNK are of a similar magnitude. Among the many new targets, we highlight the regulation of the transcriptional regulators grb10-interacting GYF protein 1 and 2 (GIGYF1/2) by p38-dependent MAP kinase-activated protein kinase 2 (MK2) phosphorylation and 14–3–3 binding. We also show that the Golgi apparatus contains numerous substrates, and is a major target for regulation by p38 and JNK. When activated, these kinases mediate structural rearrangement of the Golgi apparatus, which positively affects protein flux through the secretory system. Our work expands on our knowledge about p38 and JNK signaling with important biological ramifications.
KW - GIGYF
KW - JNK
KW - P38
KW - Phosphorylation
KW - Stress signaling
KW - Translation and Golgi
U2 - 10.3390/ijms22179595
DO - 10.3390/ijms22179595
M3 - Journal article
C2 - 34502507
AN - SCOPUS:85114258512
VL - 22
JO - International Journal of Molecular Sciences (CD-ROM)
JF - International Journal of Molecular Sciences (CD-ROM)
SN - 1424-6783
IS - 17
M1 - 9595
ER -
ID: 280064152