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Fibrous sheath of mammalian spermatozoa

The fibrous sheath is a unique cytoskeletal structure surrounding the axoneme and outer dense fibers and defines the extent of the principal piece region of the sperm flagellum. It consists of two longitudinal columns connected by closely arrayed semicircular ribs that assemble from distal to proximal throughout spermiogenesis. The fibrous sheath is believed to influence the degree of flexibility, plane of flagellar motion, and the shape of the flagellar beat. Nearly half of the protein in fibrous sheaths isolated from mouse sperm is AKAP4. This protein and two others, AKAP3 and TAKAP‐80, have anchoring sites for cAMP‐dependent protein kinase. AKAP3 also anchors ropporin, a spermatogenic cell‐specific protein that is linked through rhophilin to the small GTPase Rho. Other proteins associated with the fibrous sheath include two enzymes in the glycolytic pathway. Glyceraldehyde 3‐phosphate dehydrogenase‐s (GAPDS) is the product of a gene expressed only in spermatogenic cells, while hexokinase type 1‐s (HK1‐S) is derived from alternative transcripts present only in spermatogenic cells. Most of the other glycolytic enzymes in sperm have unique structural or functional properties. The fibrous sheath also contains a spermatogenic cell‐specific member of the μ‐class glutathione S‐transferase family (GSTM5) and an intermediate filament‐like protein (FS39). These and other observations indicate that the fibrous sheath functions as a scaffold for proteins in signaling pathways that might be involved in regulating sperm maturation, motility, capacitation, hyperactivation, and/or acrosome reaction and for enzymes in the glycolytic pathway that provide energy for the hyperactivated motility of sperm that allows them to penetrate the zona pellucida. Microsc. Res. Tech. 61:103–115, 2003. Published 2003 Wiley‐Liss, Inc.