skip to main content
OSTI.GOV title logo U.S. Department of Energy
Office of Scientific and Technical Information

Title: Regulation of Protein Interactions by M ps O ne B inder (MOB1) Phosphorylation

; ORCiD logo; ; ; ; ; ORCiD logo;
Publication Date:
Research Org.:
Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)
Sponsoring Org.:
USDOE Office of Science (SC)
OSTI Identifier:
Resource Type:
Journal Article
Resource Relation:
Journal Name: Molecular and Cellular Proteomics; Journal Volume: 16; Journal Issue: 6
Country of Publication:
United States

Citation Formats

Xiong, Shawn, Couzens, Amber L., Kean, Michelle J., Mao, Daniel Y., Guettler, Sebastian, Kurinov, Igor, Gingras, Anne-Claude, and Sicheri, Frank. Regulation of Protein Interactions by M ps O ne B inder (MOB1) Phosphorylation. United States: N. p., 2017. Web. doi:10.1074/mcp.M117.068130.
Xiong, Shawn, Couzens, Amber L., Kean, Michelle J., Mao, Daniel Y., Guettler, Sebastian, Kurinov, Igor, Gingras, Anne-Claude, & Sicheri, Frank. Regulation of Protein Interactions by M ps O ne B inder (MOB1) Phosphorylation. United States. doi:10.1074/mcp.M117.068130.
Xiong, Shawn, Couzens, Amber L., Kean, Michelle J., Mao, Daniel Y., Guettler, Sebastian, Kurinov, Igor, Gingras, Anne-Claude, and Sicheri, Frank. Mon . "Regulation of Protein Interactions by M ps O ne B inder (MOB1) Phosphorylation". United States. doi:10.1074/mcp.M117.068130.
title = {Regulation of Protein Interactions by M ps O ne B inder (MOB1) Phosphorylation},
author = {Xiong, Shawn and Couzens, Amber L. and Kean, Michelle J. and Mao, Daniel Y. and Guettler, Sebastian and Kurinov, Igor and Gingras, Anne-Claude and Sicheri, Frank},
abstractNote = {},
doi = {10.1074/mcp.M117.068130},
journal = {Molecular and Cellular Proteomics},
number = 6,
volume = 16,
place = {United States},
year = {Mon Apr 03 00:00:00 EDT 2017},
month = {Mon Apr 03 00:00:00 EDT 2017}
  • 1,25-Dihydroxyvitamin D{sub 3} (VD{sub 3}) induces differentiation in a number of leukemia cell lines and under various conditions is able to either stimulate or inhibit nuclear factor kappa B (NF-{kappa}B) activity. Here we report a time-dependent biphasic regulation of NF-{kappa}B in VD{sub 3}-treated HL-60 leukemia cells. After VD{sub 3} treatment there was an early {approx} 4 h suppression and a late 8-72 h prolonged reactivation of NF-{kappa}B. The reactivation of NF-{kappa}B was concomitant with increased IKK activities, IKK-mediated I{kappa}B{alpha} phosphorylation, p65 phosphorylation at residues S276 and S536, p65 nuclear translocation and p65 recruitment to the NF-{kappa}B/vitamin D responsive element promoters.more » In parallel with NF-{kappa}B stimulation, there was an up-regulation of NF-{kappa}B controlled inflammatory and anti-apoptotic genes such as TNF{alpha}, IL-1{beta} and Bcl-xL. VD{sub 3}-triggered reactivation of NF-{kappa}B was associated with PI3K/Akt phosphorylation. PI3K/Akt antagonists suppressed VD{sub 3}-stimulated I{kappa}B{alpha} phosphorylation as well as NF-{kappa}B-controlled gene expression. The early {approx} 4 h VD{sub 3}-mediated NF-{kappa}B suppression coincided with a prolonged increase of I{kappa}B{alpha} protein which require de novo protein synthesis, lasted for as least 72 h and was insensitive to MAPK, IKK or PI3K/Akt inhibitors. Our data suggest a novel biphasic regulation of NF-{kappa}B in VD{sub 3}-treated leukemia cells and our results may have provided the first molecular explanation for the contradictory observations reported on VD{sub 3}-mediated immune-regulation.« less
  • The 58,000-M/sub r/ form (58K form) of the polyomavirus middle T antigen (mT) is a minor species distinguished by its phosphorylation in vivo on serine and by its efficient phosphorylation on tyrosine in immune complexes. The authors report that the tumor promoter 12-O-tetradecanoylphorbol-13-acetate (TPA), an activator of protein kinase C, rapidly stimulates phosphorylation of this mT species when added to cultures of wild-type polyomavirus-infected or polyomavirus-transformed 3T3 cells. Incubation with TPA leads to an accumulation of the 58K mT species to levels 1.5- to 5-fold higher than that in untreated cells within 15 min. TPA specifically stimulates phosphorylation of themore » 58K mT species without affecting that of the 56K species. Mapping by partial proteolysis shows that TPA-stimulated phosphorylation occurs at or near the site in 58K mT that is normally phosphorylated in the absence of TPA. A synthetic diacyl glycerol, 1-oleoyl-2-acetyl-glycerol, also specifically stimulates phosphorylation of 58K mT in vivo, while an inactive phorbol analog does not. TPA fails to induce phosphorylation of a 58K mT species encoded by certain nontransforming virus mutants with altered mT proteins that normally fail to undergo phosphorylation at the 58K site. These results indicate that the 58K form of mT is phosphorylated by or through the action of protein kinase C. TPA treatment of infected cells also leads to increased levels of 58K mT as measured in the immune complex kinase reaction, in which mT becomes phosphorylated on tyrosine by pp60/sup c-src/.« less
  • We have measured the charge changing cross sections from 10 individual beams of isotopes from 8 different nuclei between Be and Ni which were accelerated to energies from 400{endash}650 MeV nucleon{sup {minus}1} at the SATURNE Accelerator in France in 1993 and 1994. These nuclei interacted in a 1.52 g cm{sup {minus}2} thick liquid hydrogen target and the fragments were observed. This is the first use of a pure hydrogen target to measure cross sections that has a thickness approximating the amount of hydrogen traversed by cosmic rays in our Galaxy. Several of the beam charges such as {sup 9}Be, {supmore » 11}B, {sup 15}N, and {sup 22}Ne have not had their fragmentation cross sections measured previously. The cross sections from the {sup 12}C, {sup 14}N, {sup 16}O, {sup 20}Ne, {sup 56}Fe, and {sup 58}Ni beams are compared with earlier measurements by our group using a CH{sub 2} {minus} C target subtraction technique to determine the hydrogen cross sections. The overall agreement between the new measurements and the earlier measurements using CH{sub 2} {minus} C subtraction is excellent with a systematic consistency between measurements of 3{percent}{endash}5{percent}. Using these new cross sections the predictions of both the B/C and {ital Z} = (21{endash}23)/Fe ratios at {approximately}1 GeV nucleon{sup {minus}1} now agree with {ital HEAO} measurements to {approximately}1{percent}{endash}2{percent}, thus obviating the need for truncation of the exponential path length distribution path length distribution that is expected from uniform propagation models. Also, these new charge changing cross sections along with the isotopic cross sections reported in paper two of this series, define the production of cosmic-ray beryllium and boron nuclei in the galaxy and also the secondary isotopes {sup 10}Be, {sup 13}C, {sup 14}N, {sup 15}N, {sup 18}O, and all of the Fe secondary isotopes to a level of precision of 3{percent}{endash}5{percent} or better. These cross sections are important for determining the abundance of these rare isotopes and others in the cosmic-ray sources as well as tracing the detailed propagation history of cosmic rays in the Galaxy. These measurements also provide high precision cross sections for the study of the nuclear physics of the interaction process. {copyright} {ital {copyright} 1998.} {ital The American Astronomical Society}« less
  • Regulation of NIa-Pro is crucial for polyprotein processing and hence, for successful infection of potyviruses. We have examined two novel mechanisms that could regulate NIa-Pro activity. Firstly, the influence of VPg domain on the proteolytic activity of NIa-Pro was investigated. It was shown that the turnover number of the protease increases when these two domains interact (cis: two-fold; trans: seven-fold) with each other. Secondly, the protease activity of NIa-Pro could also be modulated by phosphorylation at Ser129. A mutation of this residue either to aspartate (phosphorylation-mimic) or alanine (phosphorylation-deficient) drastically reduces the protease activity. Based on these observations and molecularmore » modeling studies, we propose that interaction with VPg as well as phosphorylation of Ser129 could relay a signal through Trp143 present at the protein surface to the active site pocket by subtle conformational changes, thus modulating protease activity of NIa-Pro.« less