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Vol. 13, Issue 12, 4401-4413, December 2002
Is Required for Nuclear
Anchorage of Retinoblastoma Protein
*Department of Biological Sciences, The University of Durham,
Durham DH1 3LE, United Kingdom; and The phosphorylation-dependent anchorage of retinoblastoma protein
Rb in the nucleus is essential for its function. We show that its
pocket C domain is both necessary and sufficient for nuclear anchorage
by transiently expressing green fluorescent protein (GFP) chimeras of
Rb fragments in tissue culture cells and by extracting the cells with
hypotonic solutions. Solid phase binding assays using glutathione
S-transferase-fusion of Rb pockets A, B, and C
revealed a direct association of lamin C exclusively to pocket C. Lamina-associated polypeptide (LAP) 2 Institute of
Biochemistry and Molecular Cell Biology, Vienna Biocenter, University
of Vienna, A-1030 Vienna, Austria
, a binding partner of lamins
A/C, bound strongly to pocket C and weakly to pocket B. When LAP2
was immunoprecipitated from soluble nuclear fractions, lamins A/C and
hypophosphorylated Rb were coprecipitated efficiently. Similarly,
immunoprecipitation of expressed GFP-Rb fragments by using anti-GFP
antibodies coprecipitated LAP2, provided that pocket C was present
in the GFP chimeras. On redistribution of endogenous lamin A/C and
LAP2 into nuclear aggregates by overexpressing dominant negative
lamin mutants in tissue culture cells, Rb was also sequestered into
these aggregates. In primary skin fibroblasts, LAP2 is expressed in
a growth-dependent manner. Anchorage of hypophosphorylated Rb in the
nucleus was weakened significantly in the absence of LAP2. Together,
these data suggest that hypophosphorylated Rb is anchored in the
nucleus by the interaction of pocket C with LAP2-lamin A/C complexes.
Corresponding author. E-mail address:
c.j.hutchison{at}durham.ac.uk.
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