FIGURE 2 | The synthesis and sorting of BDNF.

A schematic showing the synthesis and sorting of brain-derived neurotrophic factor (BDNF) in a typical neuron. First synthesized in the endoplasmic reticulum (ER) (1), proBDNF (precursor of BDNF) binds to intracellular sortilin in the Golgi to facilitate proper folding of the mature domain (2). A motif in the mature domain of BDNF binds to carboxypeptidase E (CPE), an interaction that sorts BDNF into large dense core vesicles, which are a component of the regulated secretory pathway. In the absence of this motif, BDNF is sorted into the constitutive pathway. After the binary decision of sorting, BDNF is transported to the appropriate site of release, either in dendrites or in axons. Because, in some cases, the pro-domain is not cleaved intracellularly by furin or protein convertases (such as protein convertase 1, PC1) (3), proBDNF can be released by neurons. Extracellular proteases, such as metalloproteinases and plasmin, can subsequently cleave the pro-region to yield mature BDNF (mBDNF) (4). MMP, matrix metalloproteinase.

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