Tyrosyl phosphorylation and activation of the myelin basic protein kinase p44mpk during sea star oocyte maturation

Sanghera, Jasbinder S.; McNabb, Chrystal K.; Tonks, Nicholas K.; Pelech, Steven

doi:10.1016/0167-4889(91)90078-c

Cited by 35 publications

(23 citation statements)

References 25 publications

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“…Activation of MAP kinases is correlated with their phosphorylation on threonine and tyrosine residues (Ray & Sturgill, 1988;Sanghera et al, 1991). Thus, we examined the ability of SV40 to induce elevated levels of phosphorylated MAP kinase.…”

Section: Effects Of Extracellular Sv40 On the Activities Of Raf And Hmentioning

confidence: 99%

Extracellular Simian Virus 40 Induces an ERK/MAP Kinase-independent Signalling Pathway that Activates Primary Response Genes and Promotes Virus Entry

Dangoria

Breau

Anderson

et al. 1996

Journal of General Virology

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Section: Effects Of Extracellular Sv40 On the Activities Of Raf And Hmentioning

confidence: 99%

Extracellular Simian Virus 40 Induces an ERK/MAP Kinase-independent Signalling Pathway that Activates Primary Response Genes and Promotes Virus Entry

Dangoria

Breau

Anderson

et al. 1996

Journal of General Virology

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“…Rat ERK1 and ERK2 and mouse Erk-1 MAP kinases expressed in E. coli autophosphorylate on threonine, serine (mouse Erk-1), and tyrosine residues Crews et al, 1991;Seger et al, 1991;Wu et al, 1991). We tested whether MsERKI expresses a tyrosine autophosphorylation activity in E coli by probing immunoblots of recombinant MsERKI (rMsERKI) with the monoclonal anti-phosphotyrosine 36- The antibody probes are given as follows: lanes 1 and 2 contain affinitypurified rabbit polyclonal antibody raised against entire purified sea star p44 m P* (Sanghere et al, 1991); lanes 3 and 4, affinity-purified rabbit polyclonal antibody raised against subdomain III region of rat ERK1 (PFEHQTYCQRTLREIQILLGFRHENVIGIRDILRAP); lanes 5 and 6, affinity-purified rabbit polyclonal antibody raised against the carboxy terminus of rat ERK1 (PFTFDMELDDLPKERLKELIFQETARFQPG-PEAP); lanes 7 and 8, affinity-purified rabbit polyclonal antibody 691 raised against a peptide from subdomain XI of rat ERK1 (KRITVEEAL-AHPYLEQYYDPTDE) . Lanes 1, 3, 5, and 7 contain total E. coli lysate of BL21(DE3) carrying vector pET11d without insert.…”

Section: Expression Of Mserkl In E Coli and Alfalfamentioning

confidence: 99%

MsERK1: a mitogen-activated protein kinase from a flowering plant.

et al. 1993

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The induction of proliferation and differentiation in cultured mammalian cells is mediated by a cascade of protein phosphorylations. A key enzyme in this signaling pathway is mitogen-activated protein (MAP) kinase (or ERK, extracellular signal-regulated kinase). We report the recovery of a full-length cDNA clone encoding a MAP kinase from alfalfa. We have named the 44-kD protein encoded by this clone MsERK1. Recombinant MsERKl (rMsERKl), when overexpressed in fscherichia coli, is recognized by antibodies raised against MAP kinases from rat, Xenopus, and sea star and by antiphosphotyrosine antibodies. Site-directed mutagenesis of MsERKl demonstrated that Tyr-215 is either directly or indirectly responsible for recognition of the protein by anti-phosphotyrosine antibodies. Semipurified rMsERKl phosphorylated itself and a model substrate, myelin basic protein, in vitro, but the Tyr-215 mutant did neither. Genomic DNA gel blot analysis suggested that the gene that encodes MsERK1 is either a member of a small multigene family or a member of a polymorphic allelic series in alfalfa. Because MAP kinase activation has been associated with mitotic stimulation in animal systems, such an enzyme may play a role in the mitogenic induction of symbiotic root nodules on alfalfa by Rhizobium signal molecules.

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“…First, the phosphatase calcineurin and the kinase Ca 2+ /calmodulin-dependent kinase II (CamKII) are required for egg activation in multiple species (Tatone et al 1999;Markoulaki et al 2003Markoulaki et al , 2004Liu and Maller 2005;Madgwick et al 2005;Hansen et al 2006;Knott et al 2006;Mochida and Hunt 2007;Nishiyama et al 2007;Chang et al 2009;Backs et al 2010;Takeo et al 2010). Second, levels of phospho-MAPKs decrease upon egg activation in Drosophila, Xenopus, mice, and some marine invertebrates (Ferrell et al 1991;Sanghera et al 1991;Shibuya et al 1992;Kubiak et al 1993;Sackton et al 2007). This dephosphorylation inactivates the MAPKs and may thus affect phosphorylation levels of MAPK protein targets present in the egg.…”

mentioning

confidence: 99%

Phospho-Regulation Pathways During Egg Activation in Drosophila melanogaster

Krauchunas¹,

Sackton²,

Wolfner

2013

Genetics

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Egg activation is the series of events that transition a mature oocyte to an egg capable of supporting embryogenesis. Increasing evidence points toward phosphorylation as a critical regulator of these events. We used Drosophila melanogaster to investigate the relationship between known egg activation genes and phosphorylation changes that occur upon egg activation. Using the phosphorylation states of four proteins-Giant Nuclei, Young Arrest, Spindly, and Vap-33-1-as molecular markers, we showed that the egg activation genes sarah, CanB2, and cortex are required for the phospho-regulation of multiple proteins. We show that an additional egg activation gene, prage, regulates the phosphorylation state of a subset of these proteins. Finally, we show that Sarah and calcineurin are required for the Anaphase Promoting Complex/Cyclosome (APC/C)-dependent degradation of Cortex following egg activation. From these data, we present a model in which Sarah, through the activation of calcineurin, positively regulates the APC/ C at the time of egg activation, which leads to a change in phosphorylation state of numerous downstream proteins.

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Tyrosyl phosphorylation and activation of the myelin basic protein kinase p44mpk during sea star oocyte maturation

Cited by 35 publications

References 25 publications

Extracellular Simian Virus 40 Induces an ERK/MAP Kinase-independent Signalling Pathway that Activates Primary Response Genes and Promotes Virus Entry

Extracellular Simian Virus 40 Induces an ERK/MAP Kinase-independent Signalling Pathway that Activates Primary Response Genes and Promotes Virus Entry

MsERK1: a mitogen-activated protein kinase from a flowering plant.

Phospho-Regulation Pathways During Egg Activation in Drosophila melanogaster

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