Abstract
Endosomal adaptor proteins are important regulators of signaling pathways underlying many biological processes. These adaptors can integrate signals from multiple pathways via localization to specific endosomal compartments, as well as through multiple protein-protein interactions. One such adaptor protein that has been implicated in regulating signaling pathways is the adaptor protein containing a pleckstrin homology (PH) domain, phosphotyrosine-binding (PTB) domain, and leucine zipper motif 1 (APPL1). APPL1 localizes to a subset of Rab5-positive endosomes through its Bin-Amphiphysin-Rvs and PH domains, and it coordinates signaling pathways through its interaction with many signaling receptors and proteins through its PTB domain. This review discusses our current understanding of the role of APPL1 in signaling and trafficking, as well as highlights recent work into the function of APPL1 in cell migration and adhesion.
Keywords:
Rab5; cell adhesion; cell migration; endosomal sorting; protein kinase B; trafficking.
© 2017 The Author(s); published by Portland Press Limited on behalf of the Biochemical Society.
Publication types
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Review
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Research Support, N.I.H., Extramural
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Research Support, Non-U.S. Gov't
MeSH terms
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Adaptor Proteins, Signal Transducing / metabolism*
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Adaptor Proteins, Signal Transducing / physiology
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Animals
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Endosomes / metabolism
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Humans
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Protein Transport
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Signal Transduction*
Substances
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APPL1 protein, human
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Adaptor Proteins, Signal Transducing