Mek1

Bendetz-Nezer, Sarit; Seger, Rony

doi:10.1038/mp.a001505.01

Cited by 7 publications

(2 citation statements)

References 27 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…33 In order to execute its function, MEKs interact with several proteins other than ERKs, such as regulators (Raf, KSR), scaffolds (Sef, p14-MP1), cytoskeleton and membrane proteins and more. [86][87][88] Upon mitogenic stimulation, MEKs and ERKs translocate from the cytoplasm to the nucleus. 85,[89][90][91][92][93][94] Due to its NES, MEK1 is rapidly exported from the nucleus by CRM-1/ exportin-1, and thus may assistERK, 95 (and probably other proteins )in its reshutteling to the cytoplasm.…”

Section: Regulation Of Pparγ Genomic Activity By Mek1mentioning

confidence: 99%

MAPK- Kinases as Nucleo-Cytoplasmic Shuttles for PPARγ

Burgermeister¹,

Seger²

2007

Cell Cycle

Self Cite

129

View full text Add to dashboard Cite

Section: Regulation Of Pparγ Genomic Activity By Mek1mentioning

confidence: 99%

MAPK- Kinases as Nucleo-Cytoplasmic Shuttles for PPARγ

Burgermeister¹,

Seger²

2007

Cell Cycle

Self Cite

129

View full text Add to dashboard Cite

“…The 45-kDa MEK1, 46-kDa MEK2, and 43-kDa MEK1b constitute an evolutionarily conserved group of highly homologous mammalian proteins (Bendetz-Nezer and Seger 2005). Structural analysis of MEK1/2 revealed that they contain a catalytic domain, which is similar to that of other protein kinases (Ohren et al 2004).…”

mentioning

confidence: 99%

Specific phosphorylation and activation of ERK1c by MEK1b: a unique route in the ERK cascade

Shaul¹,

Gibor²,

Plotnikov³

et al. 2009

Genes Dev.

Self Cite

View full text Add to dashboard Cite

Extracellular signal-regulated kinases (ERKs) are key signaling molecules that regulate a large number of cellular processes, including mitosis. We showed previously that ERK1c, an alternatively spliced form of ERK1, facilitates mitotic Golgi fragmentation without the involvement of ERK1 and ERK2. Here we demonstrate that activation of ERK1c is mainly mediated by mitogen-activated protein kinase (MAPK)/ERK kinase 1b (MEK1b), which is an alternatively spliced form of MEK1 that was previously considered an inactive kinase. MEK1b phosphorylation and activity are preferentially stimulated by nocodazole, to induce its specific activity toward ERK1c. MEK1/2, on the other hand, preferentially target ERK1/2 in response to growth factors, such as EGF. As previously demonstrated for ERK1c, also MEK1b expression and activity are elevated during mitosis, and thereby enhance Golgi fragmentation and mitotic rate. MEK1 activity is also increased during mitosis, but this isoform facilitates mitotic progression without affecting the Golgi architecture. These results illustrate that the ERK cascade is divided into two routes: the classic MEK1/2-ERK1/2 and the splice-variant MEK1b-ERK1c, each of which regulates distinct cellular processes and thus extends the cascade specificity.[Keywords: MEK; ERK; signaling cascades; Golgi fragmentation; cell cycle] Supplemental material is available at http://www.genesdev.org.

show abstract