Stathmin protein domain
| Stathmin | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 Structure of Tubulin-Colchicine-Vinblastine: Stathmin-like domain complex | |||||||||
| Identifiers | |||||||||
| Symbol | Stathmin | ||||||||
| Pfam | PF00836 | ||||||||
| InterPro | IPR000956 | ||||||||
| PROSITE | PDOC00487 | ||||||||
| SCOP | 1sa0 | ||||||||
| SUPERFAMILY | 1sa0 | ||||||||
| |||||||||
In molecular biology, the protein domain, Stathmin is a crucial protein that regulates the cell cytoskeleton. Changes in the cytoskeleton are important because the cytoskeleton is a scaffold required for many cellular processes, such as cytoplasmic organization, cell division and cell motility.[1] More specifically, stathmin is crucial in regulating the cell cycle.[2] It is found solely in eukaryotes
Function
The function of Stathmin is to regulate the cytoskeleton of the cell. The cytoskeleton is made up of long hollow cylinders named microtubules. These microtubules are made up of alpha and beta tubulin heterodimers. The changes in cytoskeleton are known as microtubule dynamics; the addition of the tubulin subunits lead to polymerisation and their loss, depolymerisation.[1] Stathmin regulates these by promoting depolymerization of microtubules or preventing polymerization of tubulin heterodimers.[2]
Additionally, Stathmin is thought to have a role in cell signaling pathway. Stathmin is a ubiquitous phosphorylated protein which makes it act as an intracellular relay for diverse regulatory pathways,[3] functioning through a variety of second messengers.
Its phosphorylation and gene expression are regulated throughout development [4] and in response to extracellular signals regulating cell proliferation, differentiation and function.[5]
Structure
Stathmin, and the related proteins SCG10 and XB3, contain a N-terminal domain (XB3 contains an additional N-terminal hydrophobic region), a 78 amino acid coiled-coil region, and a short C-terminal domain.
References
- 1 2 Kueh HY, Mitchison TJ (August 2009). "Structural plasticity in actin and tubulin polymer dynamics". Science 325 (5943): 960–3. doi:10.1126/science.1168823. PMC 2864651. PMID 19696342.
- 1 2 Rubin CI, Atweh GF (October 2004). "The role of stathmin in the regulation of the cell cycle". J. Cell. Biochem. 93 (2): 242–50. doi:10.1002/jcb.20187. PMID 15368352.
- ↑ Maucuer A, Doye V, Sobel A (May 1990). "A single amino acid difference distinguishes the human and the rat sequences of stathmin, a ubiquitous intracellular phosphoprotein associated with cell regulations". FEBS Lett. 264 (2): 275–8. doi:10.1016/0014-5793(90)80266-L. PMID 2358074.
- ↑ Maucuer A, Moreau J, Méchali M, Sobel A (August 1993). "Stathmin gene family: phylogenetic conservation and developmental regulation in Xenopus". J. Biol. Chem. 268 (22): 16420–9. PMID 8344928.
- ↑ Doye V, Soubrier F, Bauw G, Boutterin MC, Beretta L, Koppel J, Vandekerckhove J, Sobel A (July 1989). "A single cDNA encodes two isoforms of stathmin, a developmentally regulated neuron-enriched phosphoprotein". J. Biol. Chem. 264 (21): 12134–7. PMID 2745432.
This article incorporates text from the public domain Pfam and InterPro IPR000956