Target intelligence / Profile preview

Stathmin domain-containing protein 1 (STMND1)

Target
STMND1
Molecular classification
Stathmin family protein, Tubulin-binding protein, Membrane-associated protein, Other (not classified as receptor, enzyme, etc.)
01

Overview

Stathmin domain-containing protein 1 (STMND1) is a small, evolutionarily ancient protein classified within the stathmin family. It features an N-terminal motif that is both myristoylated and palmitoylated, targeting it to cell membranes, and a stathmin-like domain (SLD) with tubulin-binding properties as well as a nuclear localization signal. STMND1 is highly expressed in multiciliated epithelial cells, where it localizes to motile cilia, plasma membranes, and nuclei. Its subcellular localization is regulated by its interaction with soluble tubulin; tubulin binding inhibits nuclear translocation of STMND1, suggesting a role as a sensor of cytoplasmic tubulin concentration. Overexpression of STMND1 increases ciliary length but may result in nuclear morphology defects. STMND1 can associate with nuclear spliceosomal proteins, pointing to a possible role in pre-mRNA processing. Despite its conserved features and cilium-related functions, STMND1 is not yet linked to specific diseases or recognized as a therapeutic pharmacological target

Other names
STMND1FLJ23152stathmin domain-containing protein 1
02

Mechanism of action

Not applicable (no drugs known to target STMND1)

03

Biological functions

Regulation of microtubule assembly (biochemically inhibits microtubule polymerization at high concentrations)Senses soluble tubulin concentrationRegulates ciliary length in multiciliated epithelial cellsPutative role in nuclear pre-mRNA processing (associates with spliceosomal proteins in nucleolar speckles)Cilium-to-nucleus communication (proposed, needs further study)
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Disease associations

Other (no direct disease associations known; stathmins generally implicated in disease but STMND1's role not established)
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Safety considerations

None described; overexpression leads to nuclear morphology defects in experimental systems but not established as a clinical concern

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