Gelsolin

Gelsolin is an

Gelsolin's activity is stimulated by calcium ions (Ca²⁺).[5] Although the protein retains its overall structural integrity in both activated and deactivated states, the S6 helical tail moves like a latch depending on the concentration of calcium ions.^[11] The C-terminal end detects the calcium concentration within the cell. When there is no Ca²⁺ present, the tail of S6 shields the actin-binding sites on one of S2's helices.^[9] When a calcium ion attaches to the S6 tail, however, it straightens, exposing the S2 actin-binding sites.^[11] The N-terminal is directly involved in the severing of actin. S2 and S3 bind to the actin before the binding of S1 severs actin-actin bonds and caps the barbed end.^[10]

Gelsolin can be inhibited by a local rise in the concentration of

As an important actin regulator, gelsolin plays a role in podosome formation (along with Arp3, cortactin, and Rho GTPases).^[12]

Gelsolin also inhibits

Actin can be cross-linked into a gel by actin cross-linking proteins. Gelsolin can turn this gel into a sol, hence the name gelsolin.

Animal studies

Research in mice suggests that gelsolin, like other actin-severing proteins, is not expressed to a significant degree until after the early

An insufficiency of gelsolin in mice has also been shown to cause increased permeability of the vascular pulmonary barrier, suggesting that gelsolin is important in the response to lung injury.[15]

Related proteins

Gelsolin-like domain
3FG7​; Villin-1 domain 6: a gelsolin-like domain. The long helix is straight, consistent with the Ca2+-activated form of gelsolin.[16]
Identifiers
Symbol	?

• Amyloid precursor protein,^[20]
• Androgen receptor,^[21]
• PTK2B,^[22] and
• VDAC1.^[13]

See also

• Plasma gelsolin
• Cortactin
• Villin
• Supervillin
• Finnish type amyloidosis

References