Maturation of nuclear lamin A involves a specific carboxy-terminal trimming, which removes the polyisoprenylation site from the precursor; implications for the structure …

K Weber, U Plessmann, P Traub - FEBS letters, 1989 - Elsevier
K Weber, U Plessmann, P Traub
FEBS letters, 1989Elsevier
Lamin A, a nuclear lamina protein of differentiated cells, is synthesized as a precursor of the
mature molecule. Protein sequencing of the carboxyterminal 14 kDa fragment shows a lack
of the last 18 residues predicted by cDNA sequencing. The carboxy-terminal proteolytic
maturation explains previous biochemical results including the loss of the polyisoprenylation
site now located to the CXXM motif at the end of the chain. This view and earlier results on
lamin B predict multiple post-translational modifications shared by lamins A and B. While …
Abstract
Lamin A, a nuclear lamina protein of differentiated cells, is synthesized as a precursor of the mature molecule. Protein sequencing of the carboxyterminal 14 kDa fragment shows a lack of the last 18 residues predicted by cDNA sequencing. The carboxy-terminal proteolytic maturation explains previous biochemical results including the loss of the polyisoprenylation site now located to the CXXM motif at the end of the chain. This view and earlier results on lamin B predict multiple post-translational modifications shared by lamins A and B. While retained by lamin B, which is present in all cells, they are lost by maturation from lamin A, which probably acts only as an additional lamina constituent in differentiated cells.
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