Vesicular transport adaptor protein

While some of the details of how these adaptor proteins achieve their trafficking specificity has been worked out, there is still much to be learned.

There are several human disorders associated with defects in components of these complexes[5][6] including Alzheimer's and Parkinson's diseases.

In AP-1 it is named γ (gamma), AP-2 has α (alpha), AP-3 has δ (delta), AP-4 has ε (epsilon) and AP-5 has ζ (zeta).

Stonins (not shown in the lead figure) are also monomers similar in some regards to GGA[4] and will also not be discussed in detail in this article.

[3] The most recent common ancestor (MRCA) of the eukaryotes must have had a mechanism for trafficking molecules between its endomembranes and organelles, and the likely identity of the adaptor complex involved has been reported.

[4] There is evidence indicating that parts of the nuclear pore complex and COPII may be evolutionarily related.

[19][a] An almost universal feature of coat assembly is the recruitment of the various adaptor complexes to the "donor" membrane by the protein Arf1.

[16] As illustrated in the accompanying image, the production of a coated vesicle is not instantaneous, and a considerable fraction of the maturation time is used by making "abortive" or "futile"[21] interactions until enough interactions occur simultaneously to allow the structure to continue to develop.

Some of these interactions are directly with AP complexes and some are indirectly with "alternative adaptors", as shown in this diagram.

[10] In some cases, post-translational modifications, such as phosphorylations (shown in the figure) are important for cargo recognition.

[6] AP-2/CCVs are involved in autosomal recessive hypercholesterolemia through the associated low-density lipoprotein receptor adapter protein 1.

There are at least 3 ways in which retromer dysfunction can contribute to brain disorders, including Alzheimer and Parkinson diseases.