Abstract
Newly synthesized lysosomal enzymes are efficiently sorted and properly targeted to lysosomes by a series of interactions involving different signals and receptors (for review, see Kornfeld and Mellman, 1989). The first recognition event occurs most likely in the Cis-Golgi and leads to the synthesis of the phosphomannosyl recognition marker. In the trans-Golgi network (TGN), this marker present on every soluble lysosomal enzyme is used as a high affinity ligand by specific receptors, thus segregating this class of proteins from those destined to be secreted by a constitutive or a regulated pathway. The ligand-receptor complexes which are formed, are then delivered via clathrin-coated vesicles to a prelysosomal/endosomal compartment where the lysosomal enzymes dissociate from their receptors. While the receptors recycle back to the Golgi, the lysosomal enzymes are packaged in lysosomes by a still poorly understood process.
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© 1992 Springer-Verlag Berlin Heidelberg
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Ludwig, T., Méresse, S., Hoflack, B. (1992). Lysosomal Enzyme Transport Between Golgi and Endosomes. In: Courtoy, P.J. (eds) Endocytosis. NATO ASI Series, vol 62. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-84295-5_25
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DOI: https://doi.org/10.1007/978-3-642-84295-5_25
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