Stathmin

STMN1
Identifiers
AliasesSTMN1, C1orf215, LAP18, Lag, OP18, PP17, PP19, PR22, SMN, stathmin 1
External IDsOMIM: 151442; MGI: 96739; HomoloGene: 4063; GeneCards: STMN1; OMA:STMN1 - orthologs
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_203401
NM_001145454
NM_005563
NM_152497
NM_203399

NM_019641

RefSeq (protein)

NP_001138926
NP_005554
NP_981944
NP_981946

NP_062615

Location (UCSC)Chr 1: 25.88 – 25.91 MbChr 4: 134.2 – 134.2 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

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

Stathmin is a highly conserved 17 kDa protein that is crucial for the regulation of 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.[5] More specifically, stathmin is crucial in regulating the cell cycle.[6] It is found solely in eukaryotes.

Its function as an important regulatory protein of microtubule dynamics has been well-characterized.[7] Eukaryotic microtubules are one of three major components of the cell's cytoskeleton. They are highly dynamic structures that continuously alternate between assembly and disassembly. Stathmin performs an important function in regulating rapid microtubule remodeling of the cytoskeleton in response to the cell's needs. Microtubules are cylindrical polymers of α,β-tubulin. Their assembly is in part determined by the concentration of free tubulin in the cytoplasm.[8]

At low concentrations of free tubulin, the growth rate at the microtubule ends is slowed and results in an increased rate of depolymerization (disassembly).[7][9]

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000117632Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000028832Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ Kueh HY, Mitchison TJ (August 2009). "Structural plasticity in actin and tubulin polymer dynamics". Science. 325 (5943): 960–3. Bibcode:2009Sci...325..960K. doi:10.1126/science.1168823. PMC 2864651. PMID 19696342.
  6. ^ Cite error: The named reference pmid15368352 was invoked but never defined (see the help page).
  7. ^ a b Jourdain L, Curmi P, Sobel A, Pantaloni D, Carlier MF (September 1997). "Stathmin: a tubulin-sequestering protein which forms a ternary T2S complex with two tubulin molecules". Biochemistry. 36 (36): 10817–21. doi:10.1021/bi971491b. PMID 9312271.
  8. ^ Clément MJ, Jourdain I, Lachkar S, Savarin P, Gigant B, Knossow M, Toma F, Sobel A, Curmi PA (November 2005). "N-terminal stathmin-like peptides bind tubulin and impede microtubule assembly". Biochemistry. 44 (44): 14616–25. doi:10.1021/bi0512492. PMID 16262261.
  9. ^ Cassimeris L (February 2002). "The oncoprotein 18/stathmin family of microtubule destabilizers". Current Opinion in Cell Biology. 14 (1): 18–24. doi:10.1016/S0955-0674(01)00289-7. PMID 11792540.