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The Acrosome-Acroplaxome-Manchette Complex and the Shaping of the Spermatid Head*

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The Acrosome-Acroplaxome-Manchette Complex and the Shaping of the Spermatid Head* Review Arch Histol Cytol, 67 (4): 271-284 (2004) The acrosome-acroplaxome-manchette complex and the shaping of the spermatid head* Abraham L. Kierszenbaum and Laura L. Tres Department of Cell Biology and Anatomical Sciences, The Sophie Davis School of Biomedical Education/ The City University of New York Medical School, New York NY 10031 USA Summary. A combination of exogenous contractile forces stack of Sertoli cell F-actin-containing hoops applied to the generated by a stack of F-actin-containing hoops embracing elongating spermatid head. A tubulobulbar complex, formed the apical region of the elongating spermatid nucleus and an by cytoplasmic processes protruding from the elongating endogenous modulating mechanism dependent on the sper- spermatid head extending into the adjacent Sertoli cell, is matid-containing acrosome-acroplaxome-manchette com- located at the concave side of the spermatid head. The tubu- plex may play a cooperative role in the shaping of the sper- lobulbar complex might provide stabilizing conditions, matid head. In addition, the manchette is a key element in together with the actin-afadin-nectin-2/nectin-3 adhesion the transport of vesicles and macromolecules to the centro- unit, to enable sustained and balanced clutching exogenous some and developing spermatid tails as well as in nucleo- forces applied during the elongation of the spermatid head. cytoplasmic transport. The proposed model of spermatid head shaping is based on: 1) currently known structural and molecular components of the F-actin hoops, the main Introduction cytoskeletal element of the Sertoli cell ectoplasmic special- izations; 2) the molecular features of acrosome biogenesis; 3) One of the major causes of male infertility is the abnormal the assembly of a subacrosomal cytoskeletal plate called the development of the spermatid into a mature and motile acroplaxome; and 4) the spatial relationship of the acro- sperm. Globozoospermia (round-headed sperm) and coiled some-acroplaxome complex with the manchette, a transient sperm tails are two severe abnormalities that lead to infer- microtubular/actin-containing structure. During acrosome tility. Globozoospermia correlates with defective acrosome biogenesis, the acroplaxome becomes the nucleation site to biogenesis and tail defects that have a disruption in the which Golgi-derived proacrosomal vescicles tether and fuse. intramanchette (IMT, Kierszenbaum, 2002) and intrafla- The acroplaxome has at least two functions: it anchors the gellar transport systems (IFT, Rosenbaum and Witman, developing acrosome to the elongating spermatid head. It 2002) of molecules to the centrosome and the developing may also provide a mechanical scaffolding plate during the tail. Recent research has provided molecular data concern- shaping of the spermatid nucleus. The plate is stabilized by a ing the impact of acrosome biogenesis on spermatid nuclear marginal ring with junctional complex characteristics, shaping, in particular on the relationship of deficient acro- adjusting to exogenous clutching forces generated by the some development and round-headed sperm. Two exam- ples are the acrosome-deficient Hrb (Kang-Decker et al., 2001; Kierszenbaum et al., 2004) and the GOPC-deficient Received September 30, 2004 (Yao et al., 2002) mice mutants. Hrb is a protein associat- *Supported by USPHS grants HD36282 (ALK) and HD36477 ed with the cytosolic surface of proacrosomal transporting (LLT) vesicles in round spermatids, and a lack of Hrb protein pre- vents the vesicles from fusing to form the acrosome. The Address for correspondence: Dr. Abraham L. Kierszenbaum, GOPC protein is localized in the trans Golgi region of Department of Cell Biology and Anatomical Sciences, CUNY round spermatids, and a lack of this protein interferes with Medical School, 138th Street and Convent Avenue, Harris Hall the transport of vesicles from the Golgi apparatus to the Suite 306, New York NY 10031 USA acrosomal sac and fusion to form the acrosome. Spermatids Phone: +1-(212) 650-6811; Fax: +1-(212) 650-6812 in both mutants share a common feature: Golgi-derived E-mail: [email protected] proacrosomal vesicles attach to and align along the 272 A.L. Kierszenbaum and L.L. Tres: acroplaxome, an actin-keratin-containing cytoskeletal plate the shaft of each tubulobulbar extension. It was proposed anchoring the developing acrosome to the nuclear envelope that the tubulobulbar-Sertoli cell ectoplasmic specialization (Kierszenbaum et al., 2003a). In the Hrb mutant, proacro- assembly may stabilize the spermatid heads undergoing somal vesicles fuse forming a flat sac, called pseudoacro- elongation (Russell, 1979). More recently, it has been pro- some, while the acroplaxome is deficient in the intermedi- posed that the tubulobulbar complex participates in both the ate filament protein called Sak57 (for spermatogenic disassembly of the ectoplasmic specializations and inter- cell/sperm-associated keratin with a molecular mass of 57 nalization of Sertoli cell-spermatid adhesion molecules kDa, Kierszenbaum et al., 1996), an ortholog of keratin 5 during spermiation (Guttman et al., 2004). (K5) (Kierszenbaum et al., 2003a). Nucleopodes, protru- From the foregoing account, it can be envisioned that an sions of the spermatid nucleus with a bulb-shaped ending exogenous contractile component, represented by Sertoli linked by a stalk to the main nuclear structure, develop at cell ectoplasmic specialization, and an endogenous compo- the Sak57/K5-deficient acroplaxome (Kierszenbaum et al., nent, represented by the acrosome-acroplaxome-manchette 2004). In the GOPC, proacrosomal vesicles are also seen complex, may interact to modulate the shaping of the sper- attached to the acroplaxome while an acrosome fails to matid head. The interaction of exogenous and endogenous develop (Yao et al., 2002). components may require a relatively stable head, a function When acrosome biogenesis is in progress, the transient presumably fulfilled by the tubulobulbar complex anchored microtubule-containing manchette develops caudally to the in the adjacent Sertoli cell. acrosome. A perinuclear ring, the insertion site of man- Details of the spermatid head shaping mechanism are not chette microtubules, assembles adjacent to the marginal fully understood but pieces of the puzzle are beginning to ring of the actoplaxome from which it is separated by a nar- emerge. In this review article, we focus on the mechanism row belt-like groove. A number of elongating spermatids of acrosome biogenesis and IMT involving the transport of from the mutant mouse azh (for abnormal sperm head- Golgi-derived vesicles containing the Rab27a/b receptor shape, Meistrich, 1993) display an abnormally constrict- and mobilized by the F-actin-dependent motor myosin Va ing manchette perinuclear ring as well as severe nuclear (Kierszenbaum et al., 2003b). These two events, together deformities at the acroplaxome site (Kierszenbaum et al., with the acroplaxome and the function of the ectoplasmic 2003a). In addition, spermatids and sperm from the azh specializations of the adjacent Sertoli cell, suggest a poten- mutant mouse have a lasso-like coiled tail with a high fre- tial mechanism of spermatid head shaping based on obser- quency of head dislocation and decapitation (Mochida et vations in mouse mutants displaying globozoospermia. It al., 1999; Kierszenbaum and Tres, 2002). A non-functional should be noted that in addition to vesicle transport, Hook-1 gene, predominantly expressed in azh spermatids, cytosol-derived protein cargos bound to protein rafts can be has been proposed as being responsible for the azh abnor- mobilized by molecular motors by IMT (see Kierszenbaum, mal spermatid and sperm phenotype (Mendoza-Lujambio et 2002). Therefore, both vesicle and protein cargo transport al., 2002). The presence of the Hook-1 protein, which is might take place simultaneously within the manchette and truncated in the azh mutant, appears to establish a link along the axoneme. between the membrane of vesicles and microtubules. Spermatids develop a tubulobulbar complex at the con- cave side of the elongating head, which projects into The Rab27a/b-MyRIP-myosin Va complex and matching infoldings of the adjacent Sertoli cells (Russell organelle transport and Clermont, 1976). Each tubular element of the tubu- lobulbar complex is cuffed by F-actin bundles; each bulbar Acrosome biogenesis consists of the transport of Golgi- element is associated to a piece of the Sertoli cell endoplas- derived vesicles containing acrosomal hydrolytic proteins mic reticulum (Guttman et al., 2004). The Sertoli cell region to the acrosomal sac, which is associated to one of the poles associated with the tubulobulbar complex can be regarded of the spermatid nucleus. The opposite pole of the nucleus as a confined modification of Sertoli cell ectoplasmic spe- harbors the centrosome, which gives rise to the axoneme, cializations, consisting of the plasma membrane, harboring one of the components of the developing spermatid tail. the afadin/nectin-2 complex (Mueller et al., 2003; Guttman The transport of proacrosomal vesicles requires micro- et al., 2004), F-actin bundles and associated cisternae of the tubule-based and actin-based motor proteins (kinesin/dynein endoplasmic reticulum as predominant elements. A clear and myosin Va, respectively). Vesicles transported by the distinction is the planar arrangement of Sertoli cell ecto- myosin Va motor require three elements: a vesicle receptor plasmic specializations at the convex side of the elongating (Rab27a/b),
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