To date, little is known either about the physical interactions of heat shock protein 10 (Hsp10) with otherproteins within the cell or its involvement in signal transduction pathways. Hsp10 has been considered mainly as apartner of Hsp60 in the Hsp60/10 protein folding machine. Only recently, Hsp10 was reported to interact with proteinsinvolved 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, Hsp10expression can be up-regulated in cancer cells, because it accumulates as the cell transformation progresses. Recentdata suggest that Hsp10 may be not only a component of the folding machine but also an active player of the cellsignaling network, influencing cell cycle, nucleocytoplasmic transport, and metabolism, with putative roles in the lackof cell differentiation and in the inhibition of apoptosis. In this review, we revise the involvement of Hsp10 in signaltransduction pathways and its possible role in cancer etiology.
|Numero di pagine||8|
|Rivista||CELL STRESS & CHAPERONES|
|Stato di pubblicazione||Published - 2006|
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