Isolation of nuclear pore complexes in association with a lamina.

AUTOR(ES)

Aaronson, R P

RESUMO

Nuclear pore complexes have been isolated in association with a 150 A thick lamina by detergent and salt fractionation of nuclear envelopes from rat liver. The pore complexes exhibit characteristic morphology and appear to be attached in a highly specific orientation to the lamina, which extends over relatively large areas. The pore complex-lamina fraction is composed of three major and several minor polypeptides with little or no DNA, RNA, or phospholipid. It is suggested that the association of the pore complexes and the lamina reflects the structural arrangement of the nuclear periphery in vivo.

Documentos Relacionados

• Protein kinase activity associated with the nuclear lamina.
• Nucleoplasmic localization of prelamin A: implications for prenylation-dependent lamin A assembly into the nuclear lamina.
• Kinetic analysis of translocation through nuclear pore complexes
• Polarized integrin mediates human keratinocyte adhesion to basal lamina.
• Imaging of single-molecule translocation through nuclear pore complexes