Endoplasmic Reticulum-resident Heat Shock Protein 90 (HSP90) Isoform Glucose-regulated Protein 94 (GRP94) Regulates Cell Polarity and Cancer Cell Migration by Affecting Intracellular Transport.

Ghosh, Suman; Shinogle, Heather E; Galeva, Nadezhda A; Dobrowsky, Rick T; Blagg, Brian S J

Ghosh, Suman; Shinogle, Heather E; Galeva, Nadezhda A; Dobrowsky, Rick T; Blagg, Brian S J.

Affiliation

Ghosh S; From the Department of Medicinal Chemistry.
Shinogle HE; the Microscopy and Analytical Imaging Laboratory.
Galeva NA; the Mass Spectrometry Laboratory, and.
Dobrowsky RT; the Department of Pharmacology and Toxicology, University of Kansas, Lawrence, Kansas 66045.
Blagg BS; From the Department of Medicinal Chemistry, bblagg@ku.edu.

J Biol Chem ; 291(16): 8309-23, 2016 Apr 15.

Article in En | MEDLINE | ID: mdl-26872972

Subject(s)

Cell Movement; Cell Polarity; HSP90 Heat-Shock Proteins/metabolism; Membrane Glycoproteins/metabolism; Neoplasm Proteins/metabolism; Neoplasms/metabolism; Cell Line, Tumor; HSP90 Heat-Shock Proteins/genetics; Humans; Integrin alpha Chains/genetics; Integrin alpha Chains/metabolism; Membrane Glycoproteins/genetics; Neoplasm Proteins/genetics; Neoplasms/genetics; Neoplasms/pathology; Protein Transport; Spindle Apparatus/genetics; Spindle Apparatus/metabolism

Key words

actin; aha1; cell polarity; grp94; heat shock protein 90 (HSP90); integrin; intracellular trafficking; survivin

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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Membrane Glycoproteins / Cell Movement / Cell Polarity / HSP90 Heat-Shock Proteins / Neoplasm Proteins / Neoplasms Limits: Humans Language: En Journal: J Biol Chem Year: 2016 Type: Article

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