The reference OMIM entry for this protein is 151442

Stathmin 1; stmn1
Stathmin; smn
Leukemia-associated phosphoprotein p18; lap18
Metablastin
Op18

DESCRIPTION

Members of the stathmin family sequester tubulin (see 191130) in a ternary complex, with 2 tubulins for every stathmin-like protein. Formation of the complex interferes with microtubule dynamics in vitro and in vivo.

CLONING

Hanash et al. (1988) demonstrated an increased level of an 18-kD cytosolic phosphoprotein (p18) in the cells of various types of human acute leukemia. The cDNA that encodes p18 was cloned by Zhu et al. (1989). Sobel et al. (1989) suggested that this protein be called stathmin, from the Greek 'stathmos' (relay). By immunofluorescence microscopy, Gavet et al. (1998) detected endogenous HeLa cell stathmin expressed in a punctate cytoplasmic distribution, with staining concentrated around the nucleus. By real-time quantitative RT-PCR, Bieche et al. (2003) detected stathmin expression in all tissues examined. Expression was strongest in fetal and adult brain, spinal cord, and cerebellum, followed by thymus, bone marrow, testis, and fetal liver. Expression was intermediate in colon, ovary, placenta, uterus, and trachea, and was readily detected at substantially lower levels in all other tissues examined. Lowest expression was found in adult liver.

GENE FUNCTION

Sobel (1991) stated that stathmin is a ubiquitous, phylogenetically conserved protein present in the cytoplasm in a variety of unphosphorylated and phosphorylated forms. Its expression and phosphorylation are regulated throughout development in response to extracellular signals regulating cell proliferation, differentiation, and function. The overall pattern of its molecular forms reflects the activation of corresponding second messenger pathways. This phosphoprotein is therefore a good candidate for a general relay in signal transduction, possibly integrating diverse signals from the cell's environment. Kumar and Haugen (1994) observed that stathmin exists in bone cells and proposed that the protein may play a role in altering osteoblast growth and response to various hormonal stimuli. Maucuer et al. (1995) identified 4 mouse proteins that could interact with human stathmin in a yeast 2-hybrid screen of an embryonic mouse expression library. These included a member of the heat-shock protein family (Bip; 138120), retinoblastoma-inducible coiled-coil protein (Rb1cc1; 606837), a putative serine/threonine kinase, and a second protein with a coiled-coil structure. Using antibody directed against stathmin phosphorylated on ser16, Gavet et al. (1998) found that interphase HeLa cells were weakly stained, but mitotic cells were strongly labeled. Staining of mitotic cells increased from prophase to metaphase and decreased at cytokinesis. Analysis of synchronized cell extracts showed that phosphorylation of ser16 was detected in G2/M phases of the cell cycle. Overexpression of several phosphorylation site mutants suggested that stathmin induces depolymerization of interphase and mitotic microtubules in its unphosphorylated state, but is inactivated by phosphorylation in mitosis. Wen et al. (2010) described a potential link between stathmin and microtubule defects in spinal muscular atrophy (SMA; 253300), a motor neuron degeneration disorder caused by defects in the survival of motor neuron-1 gene (SMN1; 600354) that result in insufficient SMN protein. Stathmin was identified by proteomics analysis of Smn-knockdown NSC34 cells. Stathmin was aberrantly upregulated in vitro and in vivo, leading to a decreased level of polymerized tub ... More on the omim web site

Subscribe to this protein entry history

Jan. 22, 2019: Protein entry updated
Automatic update: OMIM entry 151442 was added.

Oct. 19, 2018: Additional information
Initial protein addition to the database. This entry was referenced in Bryk and co-workers. (2017).