Abstract：
:The HIV-1 matrix (MA) protein contains two subcellular localization signals with opposing effects. A myristoylated N-terminus governs particle assembly at the plasma membrane, and a nucleophilic motif facilitates import of the viral preintegration complex into the nucleus of nondividing cells. Here, we show that myristoylation acts as the MA dominant targeting signal in HIV-1 producer cells. During virus assembly, a subset of MA is phosphorylated on the C-terminal tyrosine by a virion-associated cellular protein kinase. Tyrosine-phosphorylated MA is then preferentially transported to the nucleus of target cells. An MA tyrosine mutant virus grows normally in dividing cells, but is blocked for nuclear import in terminally differentiated macrophages. MA tyrosine phosphorylation thus reveals the karyophilic properties of this protein within the HIV-1 preintegration complex, thereby playing a critical role for infection of nondividing cells.
journal_name
Celljournal_title
Cellauthors
Gallay P,Swingler S,Aiken C,Trono Ddoi
10.1016/0092-8674(95)90488-3subject
Has Abstractpub_date
1995-02-10 00:00:00pages
379-88issue
3eissn
0092-8674issn
1097-4172pii
0092-8674(95)90488-3journal_volume
80pub_type
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