Membrane sorting in the endocytic and phagocytic pathway of Dictyostelium discoideum

Ravanel, Kissia; Chassey, Benoı̂t de; Cornillon, Sophie; Benghezal, Mohammed; Zulianello, Laurence; Gebbie, Leigh; Letourneur, François; Cosson, Pierre

doi:10.1078/0171-9335-00215

Cited by 95 publications

(161 citation statements)

References 25 publications

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“…The rapid depletion of surface proteins from macropinosomes has previously been described in Dictyostelium (46,47). Both the plasma membrane and a perinuclear recycling pool are marked by the protein p25, which is stripped from macropinosomes within the first minutes of internalization-at the same time that WASH and retromer are active.…”

Section: Wash Drives Recycling Of Surface Proteins From Early Macropimentioning

confidence: 96%

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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Section: Wash Drives Recycling Of Surface Proteins From Early Macropimentioning

confidence: 96%

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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“…Antibodies used here were the YC1 rabbit antipeptide antiserum to a Phg1 peptide (Cornillon et al, 2000) and the H161 monoclonal antibody to the p80 endosomal marker (Ravanel et al, 2001) described previously. Anti-talin ascitis 169.477.5 was a kind gift from Prof. G. Gerisch (Martinsried, Germany).…”

Section: Antibodies and Western Blot Analysismentioning

confidence: 99%

Phg2, a Kinase Involved in Adhesion and Focal Site Modeling inDictyostelium

Gebbie

Benghezal

Cornillon

et al. 2004

MBoC

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The amoeba Dictyostelium is a simple genetic system for analyzing substrate adhesion, motility and phagocytosis. A new adhesion-defective mutant named phg2 was isolated in this system, and PHG2 encodes a novel serine/threonine kinase with a ras-binding domain. We compared the phenotype of phg2 null cells to other previously isolated adhesion mutants to evaluate the specific role of each gene product. Phg1, Phg2, myosin VII, and talin all play similar roles in cellular adhesion. Like myosin VII and talin, Phg2 also is involved in the organization of the actin cytoskeleton. In addition, phg2 mutant cells have defects in the organization of the actin cytoskeleton at the cell-substrate interface, and in cell motility. Because these last two defects are not seen in phg1, myoVII, or talin mutants, this suggests a specific role for Phg2 in the control of local actin polymerization/depolymerization. This study establishes a functional hierarchy in the roles of Phg1, Phg2, myosinVII, and talin in cellular adhesion, actin cytoskeleton organization, and motility.

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“…The p80 membrane protein was characterized previously in D. discoideum as an integral membrane protein, mostly localized to the endocytic compartments (Ravanel et al, 2001). Minor amounts of p80 can also be found at the cell surface, but it is absent from the contractile vacuole (Ravanel et al, 2001).…”

Section: P80 Endosomal Protein Is Shifted To the Cell Surface In Phg1mentioning

confidence: 99%

“…Minor amounts of p80 can also be found at the cell surface, but it is absent from the contractile vacuole (Ravanel et al, 2001). Subcellular localization of p80 was determined to detect any modifications in the intracellular transport.…”

Section: P80 Endosomal Protein Is Shifted To the Cell Surface In Phg1mentioning

confidence: 99%

“…Cells were grown on glass coverslips in HL5 medium for 3 d at 20°C and were processed for p80 immunofluorescence analysis as described previously (Ravanel et al, 2001). Briefly, cells were allowed to internalize a fluid-phase marker (fluoresbrite YG 50-nm microspheres; Polysciences) in HL5 for 90 min and then fixed in 4% paraformaldehyde, permeabilized with saponin, and incubated successively with H161 monoclonal antibody specific for the p80 endosomal protein and the corresponding fluorescent secondary antibody.…”

Section: Fluorescence Microscopymentioning

confidence: 99%

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Synergistic Control of Cellular Adhesion by Transmembrane 9 Proteins

Benghezal¹,

Cornillon²,

Gebbie³

et al. 2003

MBoC

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The transmembrane 9 (TM9) family of proteins contains numerous members in eukaryotes. Although their function remains essentially unknown in higher eukaryotes, the Dictyostelium discoideum Phg1a TM9 protein was recently reported to be essential for cellular adhesion and phagocytosis. Herein, the function of Phg1a and of a new divergent member of the TM9 family called Phg1b was further investigated in D. discoideum. The phenotypes of PHG1a, PHG1b, and PHG1a/PHG1b double knockout cells revealed that Phg1a and Phg1b proteins play a synergistic but not redundant role in cellular adhesion, phagocytosis, growth, and development. Complementation analysis supports a synergistic regulatory function rather than a receptor role for Phg1a and Phg1b proteins. Together, these results suggest that Phg1 proteins act as regulators of cellular adhesion, possibly by controlling the intracellular transport in the endocytic pathway and the composition of the cell surface.

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Membrane sorting in the endocytic and phagocytic pathway of Dictyostelium discoideum

Cited by 95 publications

References 25 publications

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

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

Phg2, a Kinase Involved in Adhesion and Focal Site Modeling inDictyostelium

Synergistic Control of Cellular Adhesion by Transmembrane 9 Proteins

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