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Phox homology band 4.1/ezrin/radixin/moesin-like proteins function as molecular scaffolds that interact with cargo receptors and Ras GTPases

Ghai, Rajesh, Mobli, Mehdi, Norwood, Suzanne J., Bugarcic, Andrea, Teasdale, Rohan D., King, Glenn F., Collins, Brett M.·2011·Proceedings of the National Academy of Sciences
DOI 10.1073/pnas.1017110108
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Abstract

Following endocytosis, the fates of receptors, channels, and other transmembrane proteins are decided via specific endosomal sorting pathways, including recycling to the cell surface for continued activity. Two distinct phox-homology (PX)-domain-containing proteins, sorting nexin (SNX) 17 and SNX27, are critical regulators of recycling from endosomes to the cell surface. In this study we demonstrate that SNX17, SNX27, and SNX31 all possess a novel 4.1/ezrin/radixin/moesin (FERM)-like domain. SNX17 has been shown to bind to Asn-Pro-Xaa-Tyr (NPxY) sequences in the cytoplasmic tails of cargo such as LDL receptors and the amyloid precursor protein, and we find that both SNX17 and SNX27 display similar affinities for NPxY sorting motifs, suggesting conserved functions in endosomal recycling. Furthermore, we show for the first time that all three proteins are able to bind the Ras GTPase through their FERM-like domains. These interactions place the PX-FERM-like proteins at a hub of endosomal sorting and signaling processes. Studies of the SNX17 PX domain coupled with cellular localization experiments reveal the mechanistic basis for endosomal localization of the PX-FERM-like proteins, and structures of SNX17 and SNX27 determined by small angle X-ray scattering show that they adopt non-self-assembling, modular structures in solution. In summary, this work defines a novel family of proteins that participate in a network of interactions that will impact on both endosomal protein trafficking and compartment specific Ras signaling cascades.

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  • Through its FERM domain, SNX27 may associate with cargoes containing a NPxY or NxxY sorting motif, with a preference for sequences phosphorylated at the tyrosine residue.

    “Through its FERM domain, SNX27 may also associate with cargoes containing a NPxY or NxxY sorting motif (x refers to any residue), with SNX27 showing a preference for sequences that are phosphorylated at the tyrosine residue [29,60,61].”

    From Global identification of neuronal and astrocytic integral membrane proteins that require Retromer for their endosomal recycling (2026) · cites this paper as [61]

    The Results (page not provided) show that SNX27 and its FERM-like domain bind an APP peptide containing an NPxY motif, and the Discussion identifies NPxY cargo binding as a function of SNX27. The passages do not establish binding to NxxY motifs or a preference for tyrosine-phosphorylated sequences; the tyrosine-to-alanine test concerns a mutation, not phosphorylation. (LLM, conf=0.88)

    Experimental — accuracy not yet measured

  • 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 Ghai et al., 2011

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Citations

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Research works printed but not linked: 38

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Metadata

Authors
Ghai, R., Mobli, M., Norwood, S. J., Bugarcic, A., Teasdale, R. D., King, G. F., & Collins, B. M.
Affiliations
Institute for Molecular Bioscience, The University of Queensland, St. Lucia, Queensland 4072, Australia
Venue
Proceedings of the National Academy of Sciences
Publisher
National Academy of Sciences
Published
2011-04-21
Volume
108
Issue
19
Pages
7763-7768
ISSN
  • 0027-8424
  • 1091-6490
DOI
10.1073/pnas.1017110108
Cited by
114
References
5
Language
en

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