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Small Heat Shock Proteins in Cellular Adhesion and Migration Evidence from Plasmodium Genetics

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Small Heat Shock Proteins in Cellular Adhesion and Migration Evidence from Plasmodium Genetics COMMENTARY Cell Adhesion & Migration 6:2, 1–7; March/April 2012; G 2012 Landes Bioscience Small heat shock proteins in cellular adhesion and migration Evidence from Plasmodium genetics Georgina N. Montagna,1 Kai Matuschewski1,2,* and Carlos A. Buscaglia3 1Max Planck Institute for Infection Biology; Berlin, Germany; 2Institute of Biology; Humboldt University; Berlin, Germany; 3Instituto de Investigaciones Biotecnológicas (IIB-INTECH); Universidad Nacional de San Martín; San Martín, Buenos Aires, Argentina ellular locomotion and adhesion domain of ~90 amino acid residues C critically depend on regulated (PFAM: PF00011).1-4 Variable N- and turnover of filamentous actin. C- termini flank this central domain, Biochemical data from diverse model resulting in an overall small molecular systems support a role for the family of mass, ranging from 12 to 43 kDa. HSPB small heat shock proteins (HSPBs) in molecules (1) have the tendency to form microfilament regulation. The small cha- large oligomers,2-5 (2) display classical © 2012 Landesperones could either act directly, Bioscience. through chaperone activity and suppress protein competition with the motor myosin, or aggregation6,7 and (3) associate with lipid indirectly, through modulation of actin bilayers, potentially preserving membrane depolymerizing factor/cofilin activity. integrity.8,9 The physiological importance However, a direct link between HSPBs of HSPBs is underscored by their ubi- and actin-based cellular motility remained quitous presence in all three domains of Do notto be established. distribute. In a recent experimental life, i.e., archaea, bacteria and eukarya,10,11 genetics study, we provided evidence for and by their association with a variety of regulation of Plasmodium motility by severe diseases, e.g., cataracts, myopathies, HSPB6/Hsp20. The infectious forms of dystrophies and diverse cancers.12-14 For malaria parasites, termed sporozoites, dis- instance, the founding member of this play fast and continuous substrate-depend- group, a-crystallin/HSPB4, is a major ent motility, which is largely driven by component of the vertebrate lens,15 and turnover of actin microfilaments. HSPB4 polymorphisms are associated with Sporozoite gliding locomotion is essential congenital cataract, a common cause of 16,17 Keywords: gliding motility, adhesion sites, to avoid destruction by host defense blindness in infants. cellular migration, small heat shock mechanisms and to ultimately reach a In the human genome 10 HSPB mem- 18,19 proteins, Hsp20, Plasmodium, sporozoite, hepatocyte, the target cell, where to bers can be identified, and some multi- malaria transform and replicate. Genetic ablation cellular eukaryotes, such as Arabidopsis of Plasmodium HSP20 dramatically chan- thaliana, express as many as 19 variants.20 Submitted: 01/31/12 ged sporozoite speed and substrate adhe- The precise biological functions of indi- Revised: 03/20/12 sion, resulting in impaired natural malaria vidual HSPBs, which are often develop- Accepted: 03/22/12 transmission. In this article, we discuss the mentally regulated or tissue-specific, function of Hsp20 in this fast-moving remain largely unknown. For example, http://dx.doi.org/10.4161/cam.20101 unicellular protozoan and implications for human Hsp20/HSPB6 is expressed at high *Correspondence to: Kai Matuschewski; the roles of HSPBs in adhesion and levels in all three major types of muscle, Email: [email protected] migration of eukaryotic cells. i.e., skeletal, cardiac and vascular smooth muscle, and cardiac-specific overexpression Commentary to: Montagna GN, Buscaglia CA, Münter S, Goosmann C, Frischknecht F, confers protection against ischemia/reper- 21 Brinkmann V, et al. Critical role for heat shock Introduction fusion injury. protein 20 (HSP20) in migration of malarial One biochemical activity of HSPBs sporozoites. J Biol Chem 2012; 287:2410–22; The family of small heat shock proteins deserves particular attention, namely their PMID:22139844; http://dx.doi.org/10.1074/jbc. (sHSPs; HSPBs) includes molecular mini- potential to regulate dynamics of fila- M111.302109 chaperones with a signature a-crystallin mentous (F-) actin. Indeed, an avian www.landesbioscience.com Cell Adhesion & Migration 1 ortholog of HSPB1 was isolated based on these findings establish an important in (MyoA), that are anchored to flattened its biochemical activity to suppress F-actin vivo role for HSPBs in cellular adhesion Golgi-derived cisternae, termed inner polymerization and viscosity in vitro, and and migration. membrane complex (IMC). The IMC is originally termed inhibitor of actin poly- a rigid structure, supported on its cyto- merization (IAP).22 This finding was Cell Migration of Malaria Parasites plasmic side by microtubules and a net- supported by subsequent studies with work of ill-defined filaments that extends mouse and human orthologs showing Cell migration is a highly spatially and beneath the entire surface of the parasite. that F-actin modulation is strictly depen- temporally coordinated process, typically According to the current model,36-39 dent on the phosphorylation status of involving (1) the formation of extended immobilized MyoA treads along short HSPB1.23,24 However, how HSPB1 and protrusions in the direction of migration, and dynamic F-actin transiently formed actin interact remains controversial, and which is driven by dynamic cytoskeleton in the narrow, so-called cortical, space mutually exclusive modes of action, rearrangements, and (2) the reversible between the IMC and the plasma mem- including barbed end capping of pre-exist- assembly of focal adhesion sites, which brane, which in turn interact with type I ing microfilaments,22,24 actin monomer depend on the physical and chemical transmembrane proteins belonging to the sequestration25 and chaperone-mediated nature of the substrate.32 In a variation of thrombospondin-related anonymous pro- prevention of polymerization26 have been substrate-dependent amoeboid cell move- tein (TRAP) family. TRAP family proteins proposed. Likewise, contradictory models, ment or crawling motility eukaryotic are stored in specialized secretory orga- i.e., direct inhibition of myosin/F-actin parasitic protozoa of the phylum nelles, so-called micronemes, and immedi- coupling via a troponin I motif27 and Apicomplexa display so-called gliding ately translocated onto the parasite surface indirectly via activation of actin depoly- motility.33 This rapid movement on solid in response to external stimuli. They bear a merizing factor/cofilin,28 were proposed substrates occurs without any apparent short cytoplasmic domain, which mediates to explain the efficient inhibition of flexing, undulation of the parasite body, indirect binding to the parasite cytoskele- ©smooth muscle2012 contraction by phosphory- Landesnor participation of appendages, Bioscience. such as ton, and a single or multiple copies of lated HSPB6. cilia or flagella. extracellular adhesive domains of varying An emerging issue, which is also of Apicomplexa include parasites of major specificities.36-39 Forward gliding loco- therapeutic relevance, is whether HSPB- medical and veterinary importance, e.g., motion is achieved by apical secretion, mediated actin reorganization also directly Plasmodium, Toxoplasma gondii—the etio- capping and backward translocation of shapes cellular motility. Work in neutro- logic agent of human toxoplasmosis34— TRAP family proteins, which link the phils, motile (~0.1–0.2Domm/sec) immune notand Babesia, distribute. which causes severe anemia, substrate or the target cell membrane to cells that migrate to sites of infection or cachexia, cerebral dysfunction and pulmo- the parasite surface. Recent data showed inflammation, showed that biochemical nary edema in infected cattle.35 They are that sporozoite motility is actually a interference with HSPB1 impaired che- obligate intracellular eukaryotes that discontinuous process, made up of small motaxis and exocytosis.29 However, largely actively invade host cells by developing parasite thrusts in between disengagement because of their short life-span neutrophils into highly polarized and usually elongated of focal adhesion sites and formation of are not amenable to genetic manipulation. cells. Cell migration is essential at several new ones.40 Hence, the rapid turnover rate Experimental genetics in an alternative stages during apicomplexan life cycles. In of these transient adhesion sites is directly highly motile eukaryote might therefore Plasmodium, for instance, these stages proportional to the speed of sporozoites. provide important insights into the in vivo permit parasite dissemination from the Although MyoA alone can supposedly roles of HSPBs. In a recent study, we mosquito inoculation site, breaching of provide enough force to drive motility, demonstrated that ablation of HSP20 in non-permissive biological barriers by inhibitor studies indicate that actin the unicellular eukaryote Plasmodium, the passing through the cytoplasm of host filament formation is a rate-limiting step causative agent of malaria,30 profoundly cells, host cell invasion and egress and in Plasmodium motility as well.40 Actin affected locomotion of highly motile pathogenesis.36 Extracellular gliding dynamics apparently also regulates parasite (~1–3 mm/sec) sporozoites.31 This extra- motility, cell traversal and cell invasion adhesion to substrate before and during cellular parasite stage is the contagious are thought to be strictly dependent gliding locomotion.40,42 Despite the critical
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