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J Biol Chem, Vol. 273, Issue 21, 13015-13021, May 22, 1998
From the Human Retrovirus Section, ABL-Basic Research Program,
NCI-Frederick Cancer Research and Development Center,
Frederick, Maryland 21702-1201
We have studied the intracellular localization of
poly(A)-binding protein 1 (PABP1) by indirect immunofluorescence as
well as by tagging with the green fluorescent protein (GFP) in living cells. We show that PABP1 is able to enter the nucleus. Accumulation of
PABP1 in the nuclei was observed upon transcription inhibition, suggesting that active transcription is required for PABP1 export. The
nuclear import of PABP1 is an energy-dependent process
since PABP1 fails to enter the nucleus upon ATP depletion and at low temperature. Transfection of PABP1 or PABP1-GFP resulted in
heterogeneity of intracellular distribution of the protein. In the low
expressing cells, PABP1 was localized in the cytoplasm, whereas in the
high expressors, we observed accumulation of the protein in the
nucleus. Nuclear PABP1 observed either after overexpression or after
transcription inhibition was found in speckles and colocalized with
splicing factor SC35. The ability of PABP1 to shuttle between nucleus
and cytoplasm was also shown by heterokaryon formation upon cell
fusion. Deletion mutagenesis showed that the minimal part of PABP1
retaining the ability to shuttle consists of the first two RNA-binding
domains. This mutant interacted with poly(A) RNA with high affinity and accumulated in the nucleus. Deletion mutants exhibiting reduced RNA
binding affinity did not accumulate in the nucleus. PABP1 has been
proposed to participate at various steps of mRNA utilization. Our
results suggest involvement of PABP1 in nuclear events associated with
the formation and transport of mRNP to the cytoplasm and identify a new
trafficking pattern for RNA-binding proteins.
The Human Poly(A)-binding Protein 1 Shuttles between the Nucleus
and the Cytoplasm
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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