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1. Serum deprivation inhibits the transcriptional co-activator YAP and cell growth via phosphorylation of the 130-kDa isoform of Angiomotin by the LATS1/2 protein kinases

Author:
Johnson, Derrick E.,   et al.   ; Adler, Jacob J.; Heller, Brigitte L.; Bringman, Lauren R.; Ranahan, William P.; Conwell, Michael D.; Sun, Yang; Hudmon, Andy; Wells, Clark D.;     Show all 9 Authors
Source:
Proceedings of the National Academy of Sciences of the United States of America 2013 v.110 no.43 pp. 17368-17373
ISSN:
0027-8424
Subject:
binding sites; blood serum; breast neoplasms; cell growth; genes; mutants; neoplasm cells; phosphorylation; protein kinases; serine; starvation; transcription (genetics); ubiquitin-protein ligase; ubiquitination
Abstract:
... Large tumor suppressor (LATS)1/2 protein kinases transmit Hippo signaling in response to intercellular contacts and serum levels to limit cell growth via the inhibition of Yes-associated protein (YAP). Here low serum and high LATS1 activity are found to enhance the levels of the 130-kDa isoform of angiomotin (Amot130) through phosphorylation by LATS1/2 at serine 175, which then forms a binding sit ...
DOI:
10.1073/pnas.1308236110
PubMed:
24101513
PubMed Central:
PMC3808603

2. A soluble α-synuclein construct forms a dynamic tetramer

Author:
Johnson, Derrick,   et al.   ; Wang, Wei; Perovic, Iva; Chittuluru, Johnathan; Kaganovich, Alice; Nguyen, Linh T. T.; Liao, Jingling; Auclair, Jared R.; Landeru, Anuradha; Simorellis, Alana K.; Ju, Shulin; Cookson, Mark R.; Asturias, Francisco J.; Agar, Jeffrey N.; Webb, Brian N.; Kang, ChulHee; Ringe, Dagmar; Petsko, Gregory A.; Pochapsky, Thomas C.; Hoang, Quyen Q.;     Show all 20 Authors
Source:
Proceedings of the National Academy of Sciences of the United States of America 2011 v.108 no.43 pp. 17797-17802
ISSN:
0027-8424
Subject:
crosslinking; humans; hydrophobicity; lipid bilayers; micelles; models; nuclear magnetic resonance spectroscopy; phospholipids; phosphorus
Abstract:
... A heterologously expressed form of the human Parkinson disease-associated protein α-synuclein with a 10-residue N-terminal extension is shown to form a stable tetramer in the absence of lipid bilayers or micelles. Sequential NMR assignments, intramonomer nuclear Overhauser effects, and circular dichroism spectra are consistent with transient formation of α-helices in the first 100 N-terminal resid ...
DOI:
10.1073/pnas.1113260108
PubMed:
22006323
PubMed Central:
PMC3203798