Other search tools

About this data

The publication data currently available has been vetted by Vanderbilt faculty, staff, administrators and trainees. The data itself is retrieved directly from NCBI's PubMed and is automatically updated on a weekly basis to ensure accuracy and completeness.

If you have any questions or comments, please contact us.

Results: 21 to 22 of 22

Publication Record

Connections

Association of brain protein phosphatase 1 with cytoskeletal targeting/regulatory subunits.
Colbran RJ, Bass MA, McNeill RB, Bollen M, Zhao S, Wadzinski BE, Strack S
(1997) J Neurochem 69: 920-9
MeSH Terms: Animals, Chromatography, Affinity, Chromatography, Gel, Chromatography, Ion Exchange, Cytoskeleton, Isoenzymes, Macromolecular Substances, Phosphoprotein Phosphatases, Prosencephalon, Protein Phosphatase 1, Rats, Subcellular Fractions, Synapses
Show Abstract · Added December 10, 2013
Protein phosphatase 1 catalytic subunit (PP1C) is highly enriched in isolated rat postsynaptic densities. Gel overlay analyses using digoxigenin (DIG)-labeled PP1C revealed four major rat brain PP1C-binding proteins (PP1bps) with molecular masses of approximately 216, 175, 134, and 75 kDa, which were (1) more abundant in brain than other rat tissues; (2) differentially expressed in microdissected brain regions; and (3) enriched in isolated cortex postsynaptic densities. PP1bp175, PP1bp134, PP1bp75, and PP1C were partially released from forebrain particulate extracts by incubation at low ionic strength, which destabilizes the actin cytoskeleton. Size-exclusion chromatography of solubilized extracts separated two main PP1 activities (approximately 600 and approximately 100 kDa). PP1bps and PP1C gamma1 were enriched in the approximately 600-kDa peak, but PP1C beta was enriched in the approximately 100-kDa peak. Furthermore, PP1bp175 and PP1bp134 exhibited lower binding of recombinant DIG-PP1C beta than recombinant DIG-PP1C gamma1 or DIG-PP1C alpha. Solubilized PP1bp175 and PP1bp134 interact with PP1C under native conditions, because they both (1) coeluted from size-exclusion and ion-exchange columns; (2) bound to microcystin-LR-Sepharose; and (3) coprecipitated using PP1C antibodies. Trypsinolysis of the approximately 600-kDa form of PP1 increased phosphorylase a phosphatase activity approximately fourfold, suggesting that interaction of PP1C with these PP1bps modulates its activity. Thus, brain PP1 activity is likely targeted to the cytoskeleton, including postsynaptic densities, by isoform-selective binding of PP1C to these targeting/regulatory subunits, contributing to the specificity of its physiological roles.
0 Communities
1 Members
0 Resources
13 MeSH Terms
Multiplicity of protein serine-threonine phosphatases in PC12 pheochromocytoma and FTO-2B hepatoma cells.
Wadzinski BE, Heasley LE, Johnson GL
(1990) J Biol Chem 265: 21504-8
MeSH Terms: Adrenal Gland Neoplasms, Amino Acid Sequence, Animals, Base Sequence, Clone Cells, Cloning, Molecular, Humans, In Vitro Techniques, Liver Neoplasms, Liver Neoplasms, Experimental, Molecular Sequence Data, Peptide Fragments, Pheochromocytoma, Phosphoprotein Phosphatases, Polymerase Chain Reaction, Protein Phosphatase 1, Protein Phosphatase 2, Rats, Tumor Cells, Cultured
Show Abstract · Added December 10, 2013
Protein purification and molecular cloning have defined five classes of protein serine-threonine phosphatase catalytic subunits referred to as types 1, 2A, 2B (calcineurin), 2C, and X. Protein serine-threonine phosphatases 1, 2A, 2B, and X appear to have significant sequence homologies, whereas the 2C enzyme is more divergent. We have used the polymerase chain reaction to define the multiplicity of the closely related types 1, 2A, 2B, and X phosphatase catalytic subunits in two clonal cell lines, rat PC12 pheochromocytoma and rat FTO-2B hepatoma. RNAs for all four related phosphatase types were expressed in both cell lines. In addition to the phosphatase X enzyme, four phosphatase 1, two phosphatase 2A, and three phosphatase 2B isoforms were identified in PC12 and FTO-2B cells. The results indicate a large multiplicity of protein serine-threonine phosphatases within clonal cells of different tissue origin, suggesting that their role in cell regulation will be as divergent as that for the protein serine-threonine kinases.
0 Communities
1 Members
0 Resources
19 MeSH Terms