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A Conserved Family of Enzymes That Phosphorylate Inositol Hexakisphosphate
A previously uncharacterized class of inositol pyrophosphate synthase is reported and it is identical to yeast Vip1 and Asp1 proteins, regulators of actin-related protein-2/3 (ARP 2/3) complexes.
PHAS-I as a link between mitogen-activated protein kinase and translation initiation.
Results obtained with antibodies, immobilized PHAS-I, and a messenger RNA cap affinity resin indicated that PHas-I did not bind eIF-4E when serine-64 was phosphorylated, indicating that PHAs-I may be a key mediator of the stimulation of protein synthesis by the diverse group of agents and stimuli that activate MAP kinase.
Mammalian septins regulate microtubule stability through interaction with the microtubule-binding protein MAP4.
Using RNA interference, this work finds that suppression of septin expression in HeLa cells caused a pronounced increase in microtubule stability, and identifies a novel molecular function for septins in mammalian cells: the modulation of microtubules dynamics through interaction with MAP4.
Smooth Muscle Phosphatase Is Regulated in Vivo by Exclusion of Phosphorylation of Threonine 696 of MYPT1 by Phosphorylation of Serine 695 in Response to Cyclic Nucleotides*
- A. Wooldridge, J. MacDonald, T. Haystead
- Biology, ChemistryJournal of Biological Chemistry
- 13 August 2004
Findings suggest a mechanism of Ca2+ desensitization in smooth muscle that involves mutual exclusion of phosphorylation, whereby phosphorylations of Ser-695 prevents phosphorylated Thr-696 and therefore inhibition of SMPP-1M.
Regulatory Interactions between the Reg1-Glc7 Protein Phosphatase and the Snf1 Protein Kinase
It is suggested that the phosphorylation ofreg1 by Snf1 is required for the release of Reg1-Glc7 from the kinase complex and also stimulates the activity of Glc7 in promoting closure of the complex.
Molecular Biologist's Guide to Proteomics
It is concluded that currently, the most practical application of proteomics is the analysis of target proteins as opposed to entire proteomes.
Activation of mitogen-activated protein kinase kinase by v-Raf in NIH 3T3 cells and in vitro.
- P. Dent, W. Haser, T. Haystead, L. A. Vincent, T. Roberts, T. Sturgill
- Biology, Computer ScienceScience
- 4 September 1992
Findings suggest that one function of c-Raf-1 in mitogenic signaling is to phosphorylate and activate MAP kinase kinase, which is activated by tyrosine and threonine phosphorylation in cells stimulated with mitogens and growth factors.
Borg proteins control septin organization and are negatively regulated by Cdc42
Borgs are the first known regulators of mammalian septin organization and provide an unexpected link between the septin and Cdc42 GTPases.
Proteomic identification of the cerebral cavernous malformation signaling complex.
It is shown for the first time that PDCD10 binds to OSM and is found in cellular CCM complexes, and OSM binds phosphatidylinositol monophosphates, which defines the targeting of the CCM complex to membranes and to proteins regulating trafficking and the cytoskeleton.