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Human cell LC-MS shows phosphorylation sites of stathmin

ABSTRACT: HIV gp120-induced stathmin phosphorylation peptide sequences identified by mass spectrometry in the proteins immunoprecipitated from stathmin-GFP expressed cell lysates with the GFP-beads.

INSTRUMENT(S): LTQ Orbitrap Elite

ORGANISM(S): Homo Sapiens (human)

SUBMITTER: Wei Xie

LAB HEAD: Jun Zhou

PROVIDER: PXD023868 | Pride | 2021-09-10

REPOSITORIES: Pride

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Publications

HIV-1 exposure promotes PKG1-mediated phosphorylation and degradation of stathmin to increase epithelial barrier permeability.

Xie Wei W Chen Mingzhen M Zhai Zhaodong Z Li Hongjie H Song Ting T Zhu Yigao Y Dong Dan D Zhou Peng P Duan Liangwei L Zhang You Y Li Dengwen D Liu Xinqi X Zhou Jun J Liu Min M

The Journal of biological chemistry 20210101

Exposure of mucosal epithelial cells to the human immunodeficiency virus type 1 (HIV-1) envelope glycoprotein gp120 is known to disrupt epithelial cell junctions by impairing stathmin-mediated microtubule depolymerization. However, the pathological significance of this process and its underlying molecular mechanism remain unclear. Here we show that treatment of epithelial cells with pseudotyped HIV-1 viral particles or recombinant gp120 protein results in the activation of protein kinase G 1 (PK ...[more]

PMID: 33839152

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