Intramanchette transport (IMT): managing the making of the spermatid head, centrosome, and tail.
Intramanchette transport (IMT) and intraflagellar transport (IFT) share similar molecular components: a raft protein complex transporting cargo proteins mobilized along microtubules by molecular motors. IFT, initially discovered in flagella of Chlamydomonas, has been also observed in cilia of the worm Caenorhabditis elegans and in mouse ciliated and flagellated cells. IFT has been defined as the mechanism by which protein raft components (also called IFT particles) are displaced between the flagellum and the plasma membrane in the anterograde direction by kinesin-II and in the retrograde direction by cytoplasmic dynein 1b. Mutation of the gene Tg737, encoding one of the components of the raft protein complex, designated Polaris in the mouse and IFT88 in both Chlamydomonas and mouse, results in defective ciliogenesis and flagellar development as well as asymmetry in left-right axis determination. Polaris/IFT88 is detected in the manchette of mouse and rat spermatids. Indications of an IMT mechanism originated from the finding that two proteins associated with the manchette (Sak57/K5 and TBP-1, the latter a component of the 26S proteasome) repositioned to the centrosome and sperm tail once the manchette disassembled. IMT has the features of the IFT machinery but, in addition, facilitates nucleocytoplasmic exchange activities during spermiogenesis. An example is Ran, a small GTPase present in the nucleus and cytoplasm of round spermatids and in the manchette of elongating spermatids. Upon disassembly of the manchette, Ran GTPase is found in the centrosome region of elongating spermatids. Because defective molecular motors and raft proteins result in defective flagella, cilia, and cilia-containing photoreceptor cells in the retina, IMT and IFT are emerging as essential mechanisms for managing critical aspects of sperm development. Details of specific role of Ran GTPase in nucleocytoplasmic transport and its relocation from the manchette to the centrosome to the sperm tail await elucidation.
Kierszenbaum
Abraham L
AL
Department of Cell Biology and Anatomical Sciences, The City University of New York Medical School, New York, New York 10031, USA. kier@med.cuny.edu
D000818:Animals; D017173:Caenorhabditis elegans / Q000502:physiology / Q000648:ultrastructure; D002467:Cell Nucleus / Q000648:ultrastructure; D018385:Centrosome / Q000378:metabolism* / Q000648:ultrastructure; D002696:Chlamydomonas / Q000502:physiology / Q000648:ultrastructure; D008297:Male; D008870:Microtubules / Q000502:physiology*; D020409:Molecular Motor Proteins / Q000502:physiology; D009024:Morphogenesis; D021381:Protein Transport / Q000502:physiology*; D011506:Proteins / Q000502:physiology; D013077:Sperm Head / Q000378:metabolism* / Q000648:ultrastructure; D013082:Sperm Tail / Q000378:metabolism* / Q000648:ultrastructure; D013091:Spermatogenesis; D025521:Tumor Suppressor Proteins; D020931:ran GTP-Binding Protein / Q000502:physiology
D020409:Molecular Motor Proteins; D011506:Proteins; C490898:Tg737Rpw protein, mouse; D025521:Tumor Suppressor Proteins; D020931:ran GTP-Binding Protein