Cell
Volume 64, Issue 1, 11 January 1991, Pages 109-121
Journal home page for Cell

Article
Network antibodies identify nuclear lamin B as a physiological attachment site for peripherin intermediate filaments

https://doi.org/10.1016/0092-8674(91)90213-IGet rights and content

Abstract

We studied the molecular associations between peripherin (a neuronal, type III intermedlate filament subunit) and nuclear lamins. We show here that isolated peripherin binds selectively to mammalian lamin B under in vitro conditions. We further demonstrate that a synthetic peptide, representing the proximal part of peripherin's tall domain (P1), also associates with mammalian lamin B in a saturable, cooperative, and specific fashion. Laboratory animals immunized with P1 spontaneously develop idlotypic and anti-idlotypic antibodies recognizing peripherin and lamin B, respectively. These data provide essentially in vivo evidence that lamin B represents a constitutive nuclear “receptor” site for the tail domains of peripherin intermediate filaments.

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      Citation Excerpt :

      Furthermore, whole-mount EM on nuclear matrix preparations in different cell types has strongly suggested that indeed the cytoplasmic IFs form a continuous network with the nuclear lamina meshwork and that they could also connect to the nuclear pores via short, ∼5-nm-thick fibers (Capco et al., 1982; Fey et al., 1984; Katsuma et al., 1987; Carmo-Fonseca et al., 1988, 1990; French et al., 1989; Fujitani et al., 1989; Wang et al., 1989). Biochemical studies have also shown that desmin, vimentin, and peripherin bind to lamin B of the karyoskeleton through their carboxy-termini (Georgatos and Blobel, 1987; Georgatos et al., 1987; Djabali et al., 1991; Papamarcaki et al., 1991). Finally, the existence of a transcellular desmin-lamin B filament network has also been reported for cardiac myocytes (Lockard and Bloom, 1993)).

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