Nuclear Translocation of Crk Adaptor Proteins by the Influenza A Virus NS1 Protein

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http://hdl.handle.net/10138/162444

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Ylosmaki , L , Fagerlund , R , Kuisma , I , Julkunen , I & Saksela , K 2016 , ' Nuclear Translocation of Crk Adaptor Proteins by the Influenza A Virus NS1 Protein ' , Viruses-Basel , vol. 8 , no. 4 , 101 . https://doi.org/10.3390/v8040101

Title: Nuclear Translocation of Crk Adaptor Proteins by the Influenza A Virus NS1 Protein
Author: Ylosmaki, Leena; Fagerlund, Riku; Kuisma, Inka; Julkunen, Ilkka; Saksela, Kalle
Contributor: University of Helsinki, Medicum
University of Helsinki, Medicum
University of Helsinki, Medicum
University of Helsinki, Medicum
Date: 2016-04
Language: eng
Number of pages: 15
Belongs to series: Viruses-Basel
ISSN: 1999-4915
URI: http://hdl.handle.net/10138/162444
Abstract: The non-structural protein-1 (NS1) of many influenza A strains, especially those of avian origin, contains an SH3 ligand motif, which binds tightly to the cellular adaptor proteins Crk (Chicken tumor virus number 10 (CT10) regulator of kinase) and Crk-like adapter protein (CrkL). This interaction has been shown to potentiate NS1-induced activation of the phosphatidylinositol 3-kinase (PI3K), but additional effects on the host cell physiology may exist. Here we show that NS1 can induce an efficient translocation of Crk proteins from the cytoplasm into the nucleus, which results in an altered pattern of nuclear protein tyrosine phosphorylation. This was not observed using NS1 proteins deficient in SH3 binding or engineered to be exclusively cytoplasmic, indicating a physical role for NS1 as a carrier in the nuclear translocation of Crk. These data further emphasize the role of Crk proteins as host cell interaction partners of NS1, and highlight the potential for host cell manipulation gained by a viral protein simply via acquiring a short SH3 binding motif.
Subject: NS1
influenza A virus
SH3 domain
Crk
virus-host interaction
C-ABL
SIGNALING COMPLEX
EXPORT SIGNAL
CYTOPLASMIC LOCALIZATION
MESSENGER-RNAS
SH3 DOMAINS
RIG-I
V-CRK
ACTIVATION
KINASE
3111 Biomedicine
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