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PIM kinases facilitate lentiviral evasion from SAMHD1 restriction via Vpx phosphorylation

ABSTRACT: Proteomic analysis revealed potential phospho-acceptor sites within Vpx by PIM3. HEK293 cells were transfected with plasmid vector encoding Vpx together with either empty vector or PIM3. Immunoprecipitated Vpx was subjected to liquid chromatography tandem-mass spectrometry.

ORGANISM(S): Homo Sapiens (human)

SUBMITTER: Akihide Ryo

PROVIDER: PXD013154 | JPOST Repository | Wed Mar 20 00:00:00 GMT 2019

REPOSITORIES: jPOST

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			Action	DRS
	150325_V175_3.mgf	Mgf
	150325_V175_3.raw	Raw
	F019474_0.csv	Csv

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PIM kinases facilitate lentiviral evasion from SAMHD1 restriction via Vpx phosphorylation.

Miyakawa Kei K Matsunaga Satoko S Yokoyama Masaru M Nomaguchi Masako M Kimura Yayoi Y Nishi Mayuko M Kimura Hirokazu H Sato Hironori H Hirano Hisashi H Tamura Tomohiko T Akari Hirofumi H Miura Tomoyuki T Adachi Akio A Sawasaki Tatsuya T Yamamoto Naoki N Ryo Akihide A

Nature communications 20190423 1

Lentiviruses have evolved to acquire an auxiliary protein Vpx to counteract the intrinsic host restriction factor SAMHD1. Although Vpx is phosphorylated, it remains unclear whether such phosphorylation indeed regulates its activity toward SAMHD1. Here we identify the PIM family of serine/threonine protein kinases as the factors responsible for the phosphorylation of Vpx and the promotion of Vpx-mediated SAMHD1 counteraction. Integrated proteomics and subsequent functional analysis reveal that PI ...[more]

PMID: 31015445

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