MAP kinase binds to the NH2‐terminal activation domain of c‐Myc

  title={MAP kinase binds to the NH2‐terminal activation domain of c‐Myc},
  author={S. Gupta and Roger J. Davis},
  journal={FEBS Letters},
  • S. GuptaR. Davis
  • Published 24 October 1994
  • Biology, Chemistry, Computer Science
  • FEBS Letters

c‐Myc transactivation domain‐associated kinases: Questionable role for map kinases in c‐Myc phosphorylation

It is concluded that Map kinases are not the in vivo kinases for Ser‐62, and phosphorylation at a different serine residue was significantly upregulated by TPA.

The Elk-1 ETS-Domain Transcription Factor Contains a Mitogen-Activated Protein Kinase Targeting Motif

It is demonstrated that the MAP kinase ERK2 is targeted to Elk-1 by a domain which is distinct from, and located N-terminally to, its phosphoacceptor motifs, which is essential for the efficient and rapid phosphorylation of Elk- 1 in vitro and full and rapid activation in vivo.

The structure of mitogen-activated protein kinase p38 at 2.1-A resolution.

The structure of mitogen-activated protein (MAP) kinase p38 has been solved at 2.1-A to an R factor of 21.0%, making p38 the second low activity MAP kinase solved to date and explaining why MAP kinases are specific for different activating enzymes, substrates, and inhibitors.

Differential targeting of MAP kinases to the ETS‐domain transcription factor Elk‐1

It is demonstrated that members of the JNK subfamily of MAPKs are also targeted to Elk‐1 by this domain, which is essential for the efficient and rapid phosphorylation and activation of Elk‐ 1 both in vitro and in vivo.

Transcription factor AP-1 regulation by mitogen-activated protein kinase signal transduction pathways

Recent progress towards understanding AP-1 regulation by the ERK, JNK, and p38 MAP kinase signal transduction pathways is reviewed.

Dual specificity phosphatases: a gene family for control of MAP kinase function

Dual specificity phosphatases are an emerging subclass of the protein tyrosine phosphatase (PTP) gene superfam‐ily, which appears to be selective for dephosphorylating the critical phosphothreonine and phosphoty‐rosine residues within MAP kinases.

MAP kinases as structural adaptors and enzymatic activators in transcription complexes

Evidence that suggests a similar bifunctional role for MAPKs in mammalian transcription complexes is reviewed, including Hog1p MAPK is stably recruited to target promoters by specific transcription factors in response to osmotic stress, and acts as both a structural adaptor and enzymatic activator driving the assembly and activation of the transcription complex.



Binding and suppression of the Myc transcriptional activation domain by p107.

The p107 protein was shown to associate with Myc in vivo and to suppress the activity of the Myc transactivation domain, and disruption of a regulatory interaction between Myc and p107 may be important in tumorigenesis.

Normal and oncogenic p21ras proteins bind to the amino-terminal regulatory domain of c-Raf-1

The Ras polypeptide and the amino-terminal regulatory domain of Raf-1 are shown to interact, directly in vitro and in a yeast expression system, and Mutations in and around the Ras effector domain impair Ras binding to Raf- 1(1-257) and Ras transforming activity in parallel.

Identification of an oncoprotein- and UV-responsive protein kinase that binds and potentiates the c-Jun activation domain.

This work has identified a serine/threonine kinase whose activity is stimulated by the same signals that stimulate the amino-terminal phosphorylation of c-Jun, and suggests a mechanism through which protein kinase cascades can specifically modulate the activity of distinct nuclear targets.

Cell cycle regulation of the c-Myc transcriptional activation domain

It is reported that the c-Myc DNA binding site confers cell cycle regulation to a reporter gene in Chinese hamster ovary cells and transactivation was biphasic with a small increase in G1 and a marked increase during the S-to-G2/M transition of the cell cycle.

ERKs, extracellular signal-regulated MAP-2 kinases.

Control of MAP kinase activation by the mitogen-induced threonine/tyrosine phosphatase PAC1

Several lines of evidence are presented indicating that PAC1 is a physiologically relevant MAP kinase phosphatase, and that Recombinant PAC1 in vitro is a dual-specific Thr/Tyr phosphat enzyme with stringent substrate specificity for MAP kinases.

Complexes of Ras.GTP with Raf-1 and mitogen-activated protein kinase kinase.

The forming of complexes containing MAPKK activity and Raf-1 protein are dependent upon the activity of Ras, and the specific interaction of activated Ras with active MAP kinase kinase (MAPKK) was confirmed by direct assays.