Identification and characterization of the nuclear import and export signals of the mammalian Ste20-like protein kinase 3.

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Citation

Lee WS, Hsu CY, Wang PL, Huang CY, Chang CH, Yuan CJ

Identification and characterization of the nuclear import and export signals of the mammalian Ste20-like protein kinase 3.

FEBS Lett. 2004 Aug 13;572(1-3):41-5.

PubMed ID
15304321 [ View in PubMed
]
Abstract

Mst3, a human Ste20-like protein kinase, has been recently demonstrated to undergo a caspase-mediated cleavage during apoptosis. The proteolytic cleavage of the C-terminus of Mst3 caused nuclear translocation of its kinase domain. This work provides evidence that Mst3 may contain a bipartite-like nuclear localization sequence (NLS) at the C-terminus of its kinase domain (residues 278-292). The removal of NLS from the kinase domain of Mst3 led to the cytoplasmic accumulation of EGFP-Mst3(Delta277). The presence of nuclear exporting signals in the Mst3 was also demonstrated by leptomycin B-treatment and serial deletion of the C-terminal regulatory domain of Mst3. A nuclear export signal was also postulated to be in the regions of amino acids 335-386. In conclusion, Mst3 contains both NLS and NES signals, which may cooperate to control the subcellular distribution of Mst3.

DrugBank Data that Cites this Article

Polypeptides
NameUniProt ID
Serine/threonine-protein kinase 24Q9Y6E0Details