The SNX-PX-BAR Family in Macropinocytosis: The Regulation of Macropinosome Formation by SNX-PX-BAR Proteins

Wang, Jack T. H.; Kerr, Markus C.; Karunaratne, Seetha; Jeanes, Angela; Yap, Alpha S.; Teasdale, Rohan D.

doi:10.1371/journal.pone.0013763

Cited by 60 publications

(54 citation statements)

References 69 publications

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“…After uptake of the receptor and its ligand, the receptor is retrieved from the phagosome to the Golgi for resecretion to the cell surface in a process that requires both the cargo-selective retromer complex and the Snx-BAR dimer Lu et al, 2011). This role is broadly similar to that of the Snx1 and Snx5 proteins in directing membrane retrieval from macropinosomes in mammalian cells (Bryant et al, 2007;Wang et al, 2010). Probably recognised by Snx27 but not retromer complex proteins.…”

Section: Wntless/mig-14 Requires Retromer For Its Retrievalmentioning

confidence: 58%

The retromer complex – endosomal protein recycling and beyond

Seaman

2012

Journal of Cell Science

414

434

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SummaryThe retromer complex is a vital element of the endosomal protein sorting machinery that is conserved across all eukaryotes. Retromer is most closely associated with the endosome-to-Golgi retrieval pathway and is necessary to maintain an active pool of hydrolase receptors in the trans-Golgi network. Recent progress in studies of retromer have identified new retromer-interacting proteins, including the WASH complex and cargo such as the Wntless/MIG-14 protein, which now extends the role of retromer beyond the endosome-to-Golgi pathway and has revealed that retromer is required for aspects of endosome-to-plasma membrane sorting and regulation of signalling events. The interactions between the retromer complex and other macromolecular protein complexes now show how endosomal protein sorting is coordinated with actin assembly and movement along microtubules, and place retromer squarely at the centre of a complex set of protein machinery that governs endosomal protein sorting. Dysregulation of retromer-mediated endosomal protein sorting leads to various pathologies, including neurodegenerative diseases such as Alzheimer disease and spastic paraplegia and the mechanisms underlying these pathologies are starting to be understood. In this Commentary, I will highlight recent advances in the understanding of retromer-mediated endosomal protein sorting and discuss how retromer contributes to a diverse set of physiological processes.

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Section: Wntless/mig-14 Requires Retromer For Its Retrievalmentioning

confidence: 58%

The retromer complex – endosomal protein recycling and beyond

Seaman

2012

Journal of Cell Science

414

434

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“…The retromer complex drives extraction of specific proteins at several trafficking steps by sequence-specific binding (37)(38)(39). The core retromer component Snx1 is also recruited to macropinosomes in mammalian cells (40,41). We therefore investigated whether Dictyostelium WASH regulates the retromer during early macropinosome maturation.…”

Section: Wash Is Recruited To Early Macropinosomes and Phagosomesmentioning

confidence: 99%

WASH drives early recycling from macropinosomes and phagosomes to maintain surface phagocytic receptors

Buckley

Gopaldass

Bosmani

et al. 2016

Proc. Natl. Acad. Sci. U.S.A.

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Macropinocytosis is an ancient mechanism that allows cells to harvest nutrients from extracellular media, which also allows immune cells to sample antigens from their surroundings. During macropinosome formation, bulk plasma membrane is internalized with all its integral proteins. It is vital for cells to salvage these proteins before degradation, but the mechanisms for sorting them are not known. Here we describe the evolutionarily conserved recruitment of the WASH (WASP and SCAR homolog) complex to both macropinosomes and phagosomes within a minute of internalization. Using Dictyostelium, we demonstrate that WASH drives protein sorting and recycling from macropinosomes and is thus essential to maintain surface receptor levels and sustain phagocytosis. WASH functionally interacts with the retromer complex at both early and late phases of macropinosome maturation, but mediates recycling via retromer-dependent and -independent pathways. WASH mutants consequently have decreased membrane levels of integrins and other surface proteins. This study reveals an important pathway enabling cells to sustain macropinocytosis without bulk degradation of plasma membrane components.phagocytosis | macropinocytosis | WASH | Dictyostelium | trafficking

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“…Recently, BAR proteins have also been reported to be involved in the formation of macropinocytic (Wang et al, 2010) and phagocytic cups (Clarke et al, 2010).…”

Section: Sculpting Of Membrane Invaginationsmentioning

confidence: 99%

Cell surface dynamics – how Rho GTPases orchestrate the interplay between the plasma membrane and the cortical cytoskeleton

Curtis

Meldolesi

2012

Journal of Cell Science

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SummarySmall GTPases are known to regulate hundreds of cell functions. In particular, Rho family GTPases are master regulators of the cytoskeleton. By regulating actin nucleation complexes, Rho GTPases control changes in cell shape, including the extension and/or retraction of surface protrusions and invaginations. Protrusion and invagination of the plasma membrane also involves the interaction between the plasma membrane and the cortical cytoskeleton. This interplay between membranes and the cytoskeleton can lead to an increase or decrease in the plasma membrane surface area and its tension as a result of the fusion (exocytosis) or internalization (endocytosis) of membranous compartments, respectively. For a long time, the cytoskeleton and plasma membrane dynamics were investigated separately. However, studies from many laboratories have now revealed that Rho GTPases, their modulation of the cytoskeleton, and membrane traffic are closely connected during the dynamic remodeling of the cell surface. Arf-and Rab-dependent exocytosis of specific vesicles contributes to the targeting of Rho GTPases and their regulatory factors to discrete sites of the plasma membrane. Rho GTPases regulate the tethering of exocytic vesicles and modulate their subsequent fusion. They also have crucial roles in the different forms of endocytosis, where they participate in the sorting of membrane domains as well as the sculpting and sealing of membrane flasks and cups. Here, we discuss how cell surface dynamics depend on the orchestration of the cytoskeleton and the plasma membrane by Rho GTPases.

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The SNX-PX-BAR Family in Macropinocytosis: The Regulation of Macropinosome Formation by SNX-PX-BAR Proteins

Cited by 60 publications

References 69 publications

The retromer complex – endosomal protein recycling and beyond

The retromer complex – endosomal protein recycling and beyond

WASH drives early recycling from macropinosomes and phagosomes to maintain surface phagocytic receptors

Cell surface dynamics – how Rho GTPases orchestrate the interplay between the plasma membrane and the cortical cytoskeleton

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