Heat shock protein 10 and signal transduction: a "capsula eburnea" of carcinogenesis?
To date, little is known either about the physical interactions of heat shock protein 10 (Hsp10) with other proteins within the cell or its involvement in signal transduction pathways. Hsp10 has been considered mainly as a partner of Hsp60 in the Hsp60/10 protein folding machine. Only recently, Hsp10 was reported to interact with proteins involved in deoxyribonucleic acid checkpoint inactivation, termination of M-phase, messenger ribonucleic acid export, import of nuclear proteins, nucleocytoplasmic transport, and pheromone signaling pathways. At the same time, Hsp10 expression can be up-regulated in cancer cells, because it accumulates as the cell transformation progresses. Recent data suggest that Hsp10 may be not only a component of the folding machine but also an active player of the cell signaling network, influencing cell cycle, nucleocytoplasmic transport, and metabolism, with putative roles in the lack of cell differentiation and in the inhibition of apoptosis. In this review, we revise the involvement of Hsp10 in signal transduction pathways and its possible role in cancer etiology.
Czarnecka
Anna M
AM
Department of Genetics, University of Warsaw, ul. Pawinskiego 5a, 02-106, Warszawa, Poland.
Campanella
Claudia
C
Zummo
Giovanni
G
Cappello
Francesco
F
D017209:Apoptosis; D018835:Chaperonin 10 / Q000378:metabolism*; D018834:Chaperonin 60 / Q000378:metabolism; D003106:Colon / Q000378:metabolism; D003110:Colonic Neoplasms / Q000378:metabolism*; D005656:Fungal Proteins / Q000378:metabolism*; D006801:Humans; D009369:Neoplasms / Q000209:etiology*; D015398:Signal Transduction
D018835:Chaperonin 10; D018834:Chaperonin 60; D005656:Fungal Proteins