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Insights into the PX (phox-homology) domain and SNX (sorting nexin) protein families: structures, functions and roles in disease

Teasdale, Rohan D., Collins, Brett M.·2012·Biochemical Journal
DOI 10.1042/bj20111226
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Abstract

The mammalian genome encodes 49 proteins that possess a PX (phox-homology) domain, responsible for membrane attachment to organelles of the secretory and endocytic system via binding of phosphoinositide lipids. The PX domain proteins, most of which are classified as SNXs (sorting nexins), constitute an extremely diverse family of molecules that play varied roles in membrane trafficking, cell signalling, membrane remodelling and organelle motility. In the present review, we present an overview of the family, incorporating recent functional and structural insights, and propose an updated classification of the proteins into distinct subfamilies on the basis of these insights. Almost all PX domain proteins bind PtdIns3P and are recruited to early endosomal membranes. Although other specificities and localizations have been reported for a select few family members, the molecular basis for binding to other lipids is still not clear. The PX domain is also emerging as an important protein–protein interaction domain, binding endocytic and exocytic machinery, transmembrane proteins and many other molecules. A comprehensive survey of the molecular interactions governed by PX proteins highlights the functional diversity of the family as trafficking cargo adaptors and membrane-associated scaffolds regulating cell signalling. Finally, we examine the mounting evidence linking PX proteins to different disorders, in particular focusing on their emerging importance in both pathogen invasion and amyloid production in Alzheimer's disease.

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  • SNX17 recruitment to endosomal compartments requires the presence of PI(3)P.

    “SNX17 recruitment to endosomal compartments requires the presence of phosphatidylinositol 3-phosphate (PI(3)P; Teasdale and Collins, 2012; Ghai et al., 2011), raising questions about whether cLTP-dependent changes in SNX17 localization are partially governed by alterations in PI(3)P.”

    From Recruitment of the SNX17-Retriever recycling pathway regulates synaptic function and plasticity (2023) · cites this paper as Teasdale and Collins, 2012

  • PI(3)P accumulation on endosomes facilitates the spatial and temporal recruitment of numerous proteins that contain PI(3)P-binding domains such as sorting nexins (SNX).

    “PI(3)P accumulation on endosomes facilitates the spatial and temporal recruitment of numerous proteins that contain PI(3)P-binding domains such as sorting nexins (SNX)5”

    From Endosomal PI(3)P regulation by the COMMD/CCDC22/CCDC93 (CCC) complex controls membrane protein recycling (2019) · cites this paper as [5]

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Metadata

Authors
Teasdale, R. D., & Collins, B. M.
Affiliations
Institute for Molecular Bioscience, University of Queensland, St. Lucia, Queensland 4072, Australia
Venue
Biochemical Journal
Publisher
Portland Press Ltd.
Published
2011-12-14
Volume
441
Issue
1
Pages
39-59
ISSN
  • 0264-6021
  • 1470-8728
DOI
10.1042/bj20111226
Cited by
281
References
13
Language
en

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