Intermediate filament 2026-11-05
An intermediate filament is a rope-like protein assembly of the cytoskeleton, typically about 10 nanometres in diameter, between an actin filament and a microtubule in thickness. Different cells use different constituent proteins: keratins reinforce many epithelial cells, vimentin forms networks in many connective-tissue cells, and lamins support the cell nucleus. Their assembled subunits do not establish the uniform head-to-tail polarity characteristic of an actin filament.[ref]
Molecular Biology of the Cell, 4th edition by Bruce Alberts and others. Chapter 16, Intermediate Filaments: structure, families and mechanical role
The mechanical role can be tested outside a biological cell. In 1991, P. A. Janmey and colleagues compared purified vimentin, actin and microtubule networks under deformation. The vimentin networks tolerated larger deformations before disruption, illustrating how an intermediate filament network can combine compliance with resistance to damage. This helps explain why load-bearing tissues need a network that can stretch rather than simply a rigid internal frame.[ref]
Viscoelastic properties of vimentin compared with other filamentous biopolymer networks by P. A. Janmey and others. Abstract and pp. 155–160, comparison of purified networks
Lamin 2026-11-05
A lamin is a type of intermediate filament protein forming part of the nuclear lamina, a network associated with the inner surface of the nuclear envelope. Lamins contribute to nuclear shape and mechanical organization and interact with components connecting the envelope to chromatin. They differ from laminin, an extracellular-matrix protein, despite the similar names. [ref]
Molecular Biology of the Cell, 4th edition by Bruce Alberts and others. Chapter 12, The Nuclear Envelope: the nuclear lamina; Chapter 16, intermediate filaments
Regulated assembly is useful during cell division. Phosphorylation of lamins helps promote lamina disassembly as the nuclear envelope breaks down in open mitosis; subsequent reassembly supports daughter nuclei. Thus a structural protein can form a load-bearing network while retaining a chemically regulated route for dismantling it.
Nuclear lamina Created 2026-10-20 Updated 2026-11-05
The nuclear lamina is a network of lamin intermediate-filament proteins associated with the inner face of the nuclear envelope in many animal cells. It supports nuclear architecture and connects the envelope with chromatin. During typical open mitosis, regulated phosphorylation promotes lamina disassembly, allowing nuclear-envelope breakdown; reassembly accompanies formation of daughter nuclei. The nuclear lamina is therefore a dynamic structural system rather than an inert shell. [ref]
Molecular Biology of the Cell, 4th edition by Bruce Alberts and others. Chapter 12, The Nuclear Envelope and Nuclear Pore Complexes; Chapter 18, Mitosis