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By John B. Lloyd (auth.), John B. Lloyd, Robert W. Mason (eds.)

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`The heterogeneity of very bold, and the result's, total, winning as a result of top of the range of the person contributions...highly recommended.'
Amercian Scientist.

`Well written and timely...of curiosity to all these taken with the learn of this organelle and for these drawn to the scientific and genetic elements of lysosomal disorders...recommended.'
Journal of scientific Genetics

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The analysis of a number of chimeric proteins between cathepsin D and pepsinogen has determined that residues 188-265 in the carboxyl lobe of cathepsin D are able to ensure M6P-independent lysosomal sorting. 1). , 1990) has been described. , 1994), the carrier proteins interacting with the M6P-independent sorting sequences in mammalian cells are still unknown. 5. VESICULAR TRANSPORT MACHINERY Targeting of lysosomal proteins is accomplished by the budding and fusion of transport vesicles. In the past few years genetic and immunolocalization studies as well as reconstituted in vitro systems have contributed to the identification of the components and the molecular mechanisms underlying vesicular transport and membrane trafficking in eukaryotic cells.

110:1923-1933. Dunn, W. , 1990b, Studies on the mechanisms of autophagy: Maturation of the autophagic vacuole, J. Cell Bio/. 110:1935-1945. , 1966, Lysosomes et endocytose, Bruxelles-Med. 46: 1053-1059. , 1994, Evidence for retrograde traffic between terminallysosomes and the prelysosomall1ate endosome compartment, J. Cell Sci. 107: 145-157. Lloyd, J. , 1976, Substrate specificity in pinocytosis and intralysosomal protein digestion, in Proteolysis and Physiological Regulation (D. W. Ribbons and K.

The GTP-bound form is incorporated into carrier vesicles budding from the donor membrane. Upon fusion of the vesicles with the acceptor membrane, rab-specific GTPase activating proteins (GAPs) promote GTP hydrolysis. , 1994; for review, see Pfeffer, 1994). Six distinct ARF proteins have been identified to date, grouped into three classes which are all able to activate cholera toxin-catalyzed ADP-ribosylation. These highly homologous proteins are modified in part at the N-terminus by myristioylation, and this is essential for activity.

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