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(Received for publication, January 23, 1997, and in revised form, May 21, 1997)
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and
From Alternative splicing of the T-cell protein
tyrosine phosphatase (TCPTP) transcript generates two forms of the
enzyme that differ at their extreme C termini: a 48-kDa endoplasmic
reticulum-associated form and a 45-kDa nuclear form. By affinity
chromatography, using GST-TCPTP fusion proteins, we have isolated three
cytoplasmic proteins of 120, 116, and 97 kDa that interact with TCPTP.
The p120 protein associated with residues 377-415 from the C terminus of the 48-kDa form of TCPTP, whereas the recognition site for p97 and
p116 was mapped to residues 350-381 encompassing the TCPTP nuclear
localization sequence (NLS). The TCPTP NLS was shown to be bipartite,
requiring basic residues 350-358 (basic cluster I) and 377-381 (basic
cluster II), the sites of interaction with p97 and p116, for efficient
nuclear translocation. The interaction between p97, p116, and the TCPTP
NLS appeared unique in that these proteins did not form a stable
interaction with the classical NLS of SV40 large T antigen or the
standard bipartite NLS of nucleoplasmin. Sequence analysis of p97
identified it as the nuclear import factor p97 (importin- Cold Spring Harbor Laboratory, Cold Spring
Harbor, New York 11724-2208 and Northwestern University Medical
School, Chicago, Illinois 60611
), which is
an essential component of the nuclear import machinery. In assays
in vitro in permeabilized cells, p97 was necessary but not
sufficient for optimal nuclear import of TCPTP. We found that TCPTP
co-immunoprecipitated with the nuclear import factor p97 from cell
lysates and that purified recombinant p97 and TCPTP interacted directly
in vitro. These results indicate selectivity in the binding
of p97 and p116 to the TCPTP NLS and suggest that p97 may mediate
events that are distinct from the classical nuclear import process.
Moreover, these results demonstrate that the C-terminal segment of
TCPTP contains docking sites for interaction with proteins that may
function to target the enzyme to defined intracellular locations and in
the process regulate TCPTP function.
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