Cytoskeleton

thumb|right|300px|The cytoskeleton consists of (a) microtubules, (b) microfilaments, and (c) intermediate filaments.

thumb|300px|Microscopy of keratin filaments inside cells

alt=Tubulin and Microtubule Metrics Infographic|thumb|

cytoskeletal structure

thumb|328px|Immunofluorescence staining pattern of vimentin antibodies. Produced by incubating vimentin primary antibodies and FITC labelled secondary antibodies with HEp-20-10 cells.

thumb|In humans, the DMD gene is located on the short (p) arm of the between positions 21.2 and 21.1 Dystrophin is a rod-shaped cytoplasmic protein, and a vital part of a protein complex that connects the cytoskeleton of a muscle fiber to the surrounding extracellular matrix through the cell membrane. This complex is variously known as the costamere or the dystrophin-associated protein complex (DAPC). Many muscle proteins, such as α-dystrobrevin, syncoilin, synemin, sarcoglycan, dystroglycan, and sarcospan, colocalize with dystrophin at the costamere. It has a molecular weight of 427 kDa.

intracellular structure that can catalyze gamma-tubulin-dependent microtubule nucleation and anchor microtubules

thumb|300px|A schematic diagram of spectrin and other cytoskeletal molecules

structural filaments in prokaryotes

Neurofilaments (NF) are classed as type IV intermediate filaments found in the cytoplasm of neurons. They are protein polymers measuring 10 nm in diameter and many micrometers in length. Together with microtubules (~25 nm) and microfilaments (7 nm), they form the neuronal cytoskeleton. They are believed to function primarily to provide structural support for axons and to regulate axon diameter, which influences nerve conduction velocity. The proteins that form neurofilaments are members of the intermediate filament protein family, which is divided into six types based on their g

mammalian protein found in Homo sapiens

The lamellipodium (: lamellipodia) (from Latin lamella, related to '', "thin sheet", and the Greek radical pod-'', "foot") is a cytoskeletal protein actin projection on the leading edge of the cell. It contains a quasi-two-dimensional actin mesh; the whole structure propels the cell across a substrate. Within the lamellipodia are ribs of actin called microspikes, which, when they spread beyond the lamellipodium frontier, are called filopodia. The lamellipodium is born of actin nucleation in the plasma membrane of the cell and is the primary area of actin incorporation or microfilament formatio

180px|thumb|This electron micrograph shows exaggerated filopodia with club-like shape induced by formin mDia2 in cultured cells. These filopodia are filled with bundled microfilament|actin filaments which were born in and converged from the lamellipodial network.

The region of a cell that lies just beneath the plasma membrane and often, but not always, contains a network of actin filaments and associated proteins.

Tonofibrils are cytoplasmic protein structures in epithelial tissues that converge at desmosomes and hemidesmosomes. They consist of bundles of keratin intermediate filaments (tonofilaments) in epithelial cells that are anchored to the cytoskeleton. They were discovered by Rudolf Heidenhain, and first described in detail by Louis-Antoine Ranvier in 1897.

Utrophin is a protein that in humans is encoded by the UTRN gene. The name is a short form for ubiquitous dystrophin. The 900 kb gene for utrophin is found on the long arm of human chromosome 6.

Loricrin is a protein that in humans is encoded by the LOR gene.

Stathmin, also known as metablastin and oncoprotein 18 is a protein that in humans is encoded by the STMN1 gene.

Crescentin is a protein which is a bacterial relative of the intermediate filaments found in eukaryotic cells. Just as tubulins and actins, the other major cytoskeletal proteins, have prokaryotic homologs in, respectively, the FtsZ and MreB proteins, intermediate filaments are linked to the crescentin protein. Some of its homologs are erroneously labelled Chromosome segregation protein ParA. This protein family is found in Caulobacter and Methylobacterium.

The microtubule organizing center in fungi; functionally homologous to the animal cell centrosome.

protein-coding gene in the species Homo sapiens

Septins are a group of GTP-binding proteins expressed in all eukaryotic cells except plants. Different septins form protein complexes with each other. These complexes can further assemble into filaments, rings and gauzes. Assembled as such, septins function in cells by localizing other proteins, either by providing a scaffold to which proteins can attach, or by forming a barrier preventing the diffusion of molecules from one compartment of the cell to another, or in the cell cortex as a barrier to the diffusion of membrane-bound proteins.

InterPro Family