Small heat shock proteins in cellular adhesion and migration

GEORGINA N. MONTAGNA; KAI MATUSCHEWSKI; CARLOS A BUSCAGLIA

Cell Adhesion and Migration

TAYLOR & FRANCIS

Año: 2012

Cellular locomotion and adhesion critically depend on regulated turnover of filamentousactin. Biochemical data from diverse model systems support a role for the family of smallheat shock proteins (HSPBs) in microfilament regulation. The small chaperones couldeither act directly, through competition with the motor myosin, or indirectly, throughmodulation of actin depolymerizing factor/cofilin activity. However, a direct linkbetween HSPBs and actin-based cellular motility remained to be established. In a recentexperimental genetics study, we provided evidence for regulation of Plasmodium motilityby HSPB6/Hsp20. The infectious forms of malaria parasites, termed sporozoites, displayfast and continuous substrate-dependent motility, which is largely driven by turnover ofactin microfilaments. Sporozoite gliding locomotion is essential to avoid destruction byhost defense mechanisms and to ultimately reach a hepatocyte, the target cell, where totransform and replicate. Genetic ablation of Plasmodium HSP20 dramatically changedsporozoite speed and substrate adhesion, resulting in impaired natural malariatransmission. In this article, we discuss the function of Hsp20 in this fast-movingunicellular protozoan and implications for the roles of HSPs in adhesion and migration ofeukaryotic cells.