title: Stathmin and its phosphoprotein family: general properties, biochemical and functional interaction with tubulin.
abstract: Stathmin, also referred to as Op18, is a ubiquitous cytosolic phosphoprotein, proposed to be a small regulatory protein and a relay integrating diverse intracellular signaling pathways involved in the control of cell proliferation, differentiation and activities. It interacts with several putative downstream target and/or partner proteins. One major action of stathmin is to interfere with microtubule dynamics, by inhibiting the formation of microtubules and/or favoring their depolymerization. Stathmin (S) interacts directly with soluble tubulin (T), which results in the formation of a T2S complex which sequesters free tubulin and therefore impedes microtubule formation. However, it has been also proposed that stathmin's action on microtubules might result from the direct promotion of catastrophes, which is still controversial. Phosphorylation of stathmin regulates its biological actions: it reduces its affinity for tubulin and hence its action on microtubule dynamics, which allows for example progression of cells through mitosis. Stathmin is also the generic element of a protein family including the neural proteins SCG10, SCLIP and RB3/RB3'/RB3". Interestingly, the stathmin-like domains of these proteins also possess a tubulin binding activity in vitro. In vivo, the transient expression of neural phosphoproteins of the stathmin family leads to their localization at Golgi membranes and, as previously described for stathmin and SCG10, to the depolymerization of interphasic microtubules. Altogether, the same mechanism for microtubule destabilization, that implies tubulin sequestration, is a common feature likely involved in the specific biological roles of each member of the stathmin family.
authors.affiliation: INSERM U440, Institut du Fer à Moulin, 17 rue du Fer à Moulin, 75005, Paris, France.
authors.forename: P A
authors.initials: PA
authors.lastname: Curmi
authors.forename: O
authors.initials: O
authors.lastname: Gavet
authors.forename: E
authors.initials: E
authors.lastname: Charbaut
authors.forename: S
authors.initials: S
authors.lastname: Ozon
authors.forename: S
authors.initials: S
authors.lastname: Lachkar-Colmerauer
authors.forename: V
authors.initials: V
authors.lastname: Manceau
authors.forename: S
authors.initials: S
authors.lastname: Siavoshian
authors.forename: A
authors.initials: A
authors.lastname: Maucuer
authors.forename: A
authors.initials: A
authors.lastname: Sobel
mesh_terms: D000818:Animals; D001665:Binding Sites; D002352:Carrier Proteins; D002454:Cell Differentiation / Q000502:physiology; D002455:Cell Division / Q000502:physiology; D006801:Humans; D008565:Membrane Proteins; D008868:Microtubule Proteins; D008870:Microtubules / Q000378:metabolism; D008954:Models, Biological; D009414:Nerve Growth Factors / Q000737:chemistry / Q000502:physiology; D009474:Neurons / Q000502:physiology; D010750:Phosphoproteins / Q000737:chemistry / Q000378:metabolism / Q000502:physiology*; D010766:Phosphorylation; D011485:Protein Binding; D050777:Stathmin; D014404:Tubulin / Q000378:metabolism*
chemical_list: D002352:Carrier Proteins; D008565:Membrane Proteins; D008868:Microtubule Proteins; D009414:Nerve Growth Factors; D010750:Phosphoproteins; C493995:STMN1 protein, human; C063314:STMN2 protein, human; C112285:STMN3 protein, human; C491795:STMN4 protein, human; D050777:Stathmin; C512848:Stmn2 protein, rat; C491792:Stmn3 protein, rat; D014404:Tubulin