Purification and characterization of mitogen-activated protein kinase activator(s) from epidermal growth factor-stimulated A431 cells.

Seger, Rony; Ahn, Natalie G.; Posada, James; Munar, Erlynda; Jensen, Amy; Cooper, Jonathan A.; Cobb, Melanie H.; Krebs, Edwin G.

doi:10.1016/s0021-9258(19)49722-6

Cited by 352 publications

(31 citation statements)

References 39 publications

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“…A MAPKK (mekl) has been purified and cloned in several laboratories Ashworth et al, 1992;Seger et al, 1992;Wu et al, 1993). To determine whether the enzymic properties of this protein are consistent with the characteristics of the in vivo phosphorylation and activation of MAP kinase described above, we analysed the phosphorylation of MAP kinase mutants using purified MAPKK in vitro.…”

Section: Phosphorylation Of Map Kinase In Vitromentioning

confidence: 99%

“…We also utilized kinasedefective variants of MAP kinase with mutations in either the ATP-binding loop or the catalytic loop, and obtained data suggesting that the activity or structure of the catalytic loop of MAP kinase plays an important role in its own dual phosphorylation. al., 1992; Kosako et al, 1992), purification Seger et al, 1992;Matsuda et al, 1992;Wu et al, 1992) and cloning Seger et al, 1992;Ashworth et al, 1992;Wu et al, 1993) of MAP kinase kinases (MAPKKs; mekl). MAPKKs appear to be dual-specificity protein kinases, capable of phosphorylating both the regulatory threonine and tyrosine residues, and hence enzymically activating p42malk and p44mavk in vitro. Dual-specificity kinases are a recently described class ofprotein kinases.…”

Section: Introductionmentioning

confidence: 99%

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Dual phosphorylation and autophosphorylation in mitogen-activated protein (MAP) kinase activation

Her

Lakhani

et al. 1993

Biochemical Journal

115

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p42mapk [mitogen activated protein (MAP) kinase; extracellular signal-regulated protein kinase (ERK)] is a serine/threonine-specific protein kinase that is activated by dual tyrosine and threonine phosphorylation in response to diverse agonists. Both the tyrosine and threonine phosphorylations are necessary for full enzymic activity. A MAP kinase activator recently purified and cloned has been shown to be a protein kinase (MAP kinase kinase) that is able to induce the dual phosphorylation of MAP kinase on both the regulatory tyrosine and threonine sites in vitro. In the present paper we have utilized MAP kinase mutants altered in the sites of regulatory phosphorylation to show, both in vivo and in vitro, that phosphorylation of the tyrosine and the threonine can occur independently of one another, with no required order of phosphorylation. We also utilized kinase-defective variants of MAP kinase with mutations in either the ATP-binding loop or the catalytic loop, and obtained data suggesting that the activity or structure of the catalytic loop of MAP kinase plays an important role in its own dual phosphorylation.

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Section: Phosphorylation Of Map Kinase In Vitromentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Dual phosphorylation and autophosphorylation in mitogen-activated protein (MAP) kinase activation

Her

Lakhani

et al. 1993

Biochemical Journal

115

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“…Our current data suggest that vault complex–dependent mvtRNA transportation in neurites may serve as a downstream signaling event of Aurora-A activation and enhance the activation of ERK in the synaptic region. MEK is a regulatory component of the MAPK signaling pathway, and its target sites for phosphorylation are very limited, with most activity directed at ERK ( Ordan et al, 2018 ; Seger et al, 1992 ; Yuan et al, 2018 ). Because previous studies have reported that vtRNA directly controls protein function, we hypothesized that mvtRNA can bind to and regulate MEK1.…”

Section: Resultsmentioning

confidence: 99%

“…10 ). MEK is a dual-specificity protein kinase that can phosphorylate both the threonine and tyrosine residues of ERK ( Seger et al, 1992 ; Yuan et al, 2018 ). Much information has been accumulated about the relationship between the structure and activity of MEK.…”

Section: Discussionmentioning

confidence: 99%

Small noncoding vault RNA modulates synapse formation by amplifying MAPK signaling

Wakatsuki

Takahashi

Shibata

et al. 2021

Journal of Cell Biology

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The small noncoding vault RNA (vtRNA) is a component of the vault complex, a ribonucleoprotein complex found in most eukaryotes. Emerging evidence suggests that vtRNAs may be involved in the regulation of a variety of cellular functions when unassociated with the vault complex. Here, we demonstrate a novel role for vtRNA in synaptogenesis. Using an in vitro synapse formation model, we show that murine vtRNA (mvtRNA) promotes synapse formation by modulating the MAPK signaling pathway. mvtRNA is transported to the distal region of neurites as part of the vault complex. Interestingly, mvtRNA is released from the vault complex in the neurite by a mitotic kinase Aurora-A–dependent phosphorylation of MVP, a major protein component of the vault complex. mvtRNA binds to and activates MEK1 and thereby enhances MEK1-mediated ERK activation in neurites. These results suggest the existence of a regulatory mechanism of the MAPK signaling pathway by vtRNAs as a new molecular basis for synapse formation.

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“…Two MAP kinases, p42maPk and p44mapk, have been well characterized in many mammalian cell systems (33,41). Both enzymes are phosphorylated on tyrosine and threonine and are activated by a novel protein kinase termed MAP kinase kinase (MKK), also known as MAP kinase/extracellular signal-regulated kinase (MEK) kinase (9,15,29,34,37). The activity of MKK is specific for the regulatory residues, threonine 183 and tyrosine 185, in p42maPk (32), suggesting that MKK is a key regulator of MAP kinases in the cell.…”

mentioning

confidence: 99%

Mitogen-Activated Protein Kinase Kinase 1 (MKK1) Is Negatively Regulated by Threonine Phosphorylation

Rossomando

Dent

Sturgill

et al. 1994

Molecular and Cellular Biology

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Mitogen-activated protein kinase kinase 1 (MKK1), a dual-specificity tyrosine/threonine protein kinase, has been shown to be phosphorylated and activated by the raf oncogene product as part of the mitogen-activated protein kinase cascade. Here we report the phosphorylation and inactivation of MKK1 by phosphorylation on threonine 286 and threonine 292. MKK1 contains a consensus phosphorylation site for p34cdc2, a serine/threonine protein kinase that regulates the cell division cycle, at Thr-286 and a related site at Thr-292. p34cdc2 catalyzes the in vitro phosphorylation of MKK1 on both of these threonine residues and inactivates MKK1 enzymatic activity. Both sites are phosphorylated in vivo as well. The data presented in this report provide evidence that MKK1 is negatively regulated by threonine phosphorylation.

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Purification and characterization of mitogen-activated protein kinase activator(s) from epidermal growth factor-stimulated A431 cells.

Cited by 352 publications

References 39 publications

Dual phosphorylation and autophosphorylation in mitogen-activated protein (MAP) kinase activation

Dual phosphorylation and autophosphorylation in mitogen-activated protein (MAP) kinase activation

Small noncoding vault RNA modulates synapse formation by amplifying MAPK signaling

Mitogen-Activated Protein Kinase Kinase 1 (MKK1) Is Negatively Regulated by Threonine Phosphorylation

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