The stress-activated protein kinase subfamily of c-Jun kinases
Identifieur interne : 004307 ( Main/Exploration ); précédent : 004306; suivant : 004308The stress-activated protein kinase subfamily of c-Jun kinases
Auteurs : John M. Kyriakis ; Papia Banerjee ; Eleni Nikolakaki ; Tianang Dai ; Elizabeth A. Rubie ; Mir F. Ahmad ; Joseph Avruch ; James R. WoodgettSource :
- Nature [ 0028-0836 ] ; 1994-05-12.
Abstract
THE mitogen-activated protein (MAP) kinases Erk-1 and Erk-2 are proline-directed kinases that are themselves activated through concomitant phosphorylation of tyrosine and threonine residues14. The kinase p54 (Mr 54,000), which was first isolated from cycloheximide-treated rats, is proline-directed like Erks-1/2, and requires both Tyr and Ser/Thr phosphorylation3,5,6 for activity. p54 is, however, distinct from Erks-1/2 in its substrate specificity, being unable to phosphon late pp90rsk but more active in phosphor-ylating the c-Jun transactivation domain5,7,8. Molecular cloning of p54 reveals a unique subfamily of extracellularly regulated kinases. Although they are 4045% identical in sequence to Erks-1/2, unlike Erks-1/2 the p54s are only poorly activated in most cells by mitogens or phorbol esters. However, p54s are the principal c-Jun N-terminal kinases activated by cellular stress and tumour necrosis factor (TNF)-, hence they are designated stress-activated protein kinases, or SAPKs. SAPKs are also activated by sphingo-myelinase, which elicits a subset of cellular responses to TNF- (ref. 9). SAPKs therefore define a new TNF- and stress-activated signalling pathway, possibly initiated by sphingomyelin-based second messengers, which regulates the activity of c-Jun.
Url:
DOI: 10.1038/369156a0
Affiliations:
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Kyriakis</name><affiliation><wicri:noCountry code="subField">(M.F.A.).</wicri:noCountry></affiliation></author><author><name sortKey="Banerjee, Papia" sort="Banerjee, Papia" uniqKey="Banerjee P" first="Papia" last="Banerjee">Papia Banerjee</name></author><author><name sortKey="Nikolakaki, Eleni" sort="Nikolakaki, Eleni" uniqKey="Nikolakaki E" first="Eleni" last="Nikolakaki">Eleni Nikolakaki</name></author><author><name sortKey="Dai, Tianang" sort="Dai, Tianang" uniqKey="Dai T" first="Tianang" last="Dai">Tianang Dai</name></author><author><name sortKey="Rubie, Elizabeth A" sort="Rubie, Elizabeth A" uniqKey="Rubie E" first="Elizabeth A." last="Rubie">Elizabeth A. Rubie</name></author><author><name sortKey="Ahmad, Mir F" sort="Ahmad, Mir F" uniqKey="Ahmad M" first="Mir F." last="Ahmad">Mir F. Ahmad</name></author><author><name sortKey="Avruch, Joseph" sort="Avruch, Joseph" uniqKey="Avruch J" first="Joseph" last="Avruch">Joseph Avruch</name><affiliation><wicri:noCountry code="subField">(M.F.A.).</wicri:noCountry></affiliation></author><author><name sortKey="Woodgett, James R" sort="Woodgett, James R" uniqKey="Woodgett J" first="James R." last="Woodgett">James R. Woodgett</name></author></analytic><monogr></monogr><series><title level="j" type="main">Nature</title><imprint><publisher>Nature Publishing Group</publisher><date when="1994-05-12">1994-05-12</date><biblScope unit="vol">369</biblScope><biblScope unit="issue">6476</biblScope><biblScope unit="page" from="156">156</biblScope><biblScope unit="page" to="160">160</biblScope><date type="Copyright" when="1994">1994</date></imprint><idno type="ISSN">0028-0836</idno></series></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0028-0836</idno></seriesStmt></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract">THE mitogen-activated protein (MAP) kinases Erk-1 and Erk-2 are proline-directed kinases that are themselves activated through concomitant phosphorylation of tyrosine and threonine residues14. The kinase p54 (Mr 54,000), which was first isolated from cycloheximide-treated rats, is proline-directed like Erks-1/2, and requires both Tyr and Ser/Thr phosphorylation3,5,6 for activity. p54 is, however, distinct from Erks-1/2 in its substrate specificity, being unable to phosphon late pp90rsk but more active in phosphor-ylating the c-Jun transactivation domain5,7,8. Molecular cloning of p54 reveals a unique subfamily of extracellularly regulated kinases. Although they are 4045% identical in sequence to Erks-1/2, unlike Erks-1/2 the p54s are only poorly activated in most cells by mitogens or phorbol esters. However, p54s are the principal c-Jun N-terminal kinases activated by cellular stress and tumour necrosis factor (TNF)-, hence they are designated stress-activated protein kinases, or SAPKs. SAPKs are also activated by sphingo-myelinase, which elicits a subset of cellular responses to TNF- (ref. 9). SAPKs therefore define a new TNF- and stress-activated signalling pathway, possibly initiated by sphingomyelin-based second messengers, which regulates the activity of c-Jun.</div></front></TEI><affiliations><list></list><tree><noCountry><name sortKey="Ahmad, Mir F" sort="Ahmad, Mir F" uniqKey="Ahmad M" first="Mir F." last="Ahmad">Mir F. Ahmad</name><name sortKey="Avruch, Joseph" sort="Avruch, Joseph" uniqKey="Avruch J" first="Joseph" last="Avruch">Joseph Avruch</name><name sortKey="Banerjee, Papia" sort="Banerjee, Papia" uniqKey="Banerjee P" first="Papia" last="Banerjee">Papia Banerjee</name><name sortKey="Dai, Tianang" sort="Dai, Tianang" uniqKey="Dai T" first="Tianang" last="Dai">Tianang Dai</name><name sortKey="Kyriakis, John M" sort="Kyriakis, John M" uniqKey="Kyriakis J" first="John M." last="Kyriakis">John M. Kyriakis</name><name sortKey="Nikolakaki, Eleni" sort="Nikolakaki, Eleni" uniqKey="Nikolakaki E" first="Eleni" last="Nikolakaki">Eleni Nikolakaki</name><name sortKey="Rubie, Elizabeth A" sort="Rubie, Elizabeth A" uniqKey="Rubie E" first="Elizabeth A." last="Rubie">Elizabeth A. Rubie</name><name sortKey="Woodgett, James R" sort="Woodgett, James R" uniqKey="Woodgett J" first="James R." last="Woodgett">James R. Woodgett</name></noCountry></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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