Three sorting nexins drive the degradation of apoptotic cells in response to PtdIns(3)P signaling

Lü, Nan; Shen, Qian; Mahoney, Tim; Li, Xianghua; Zhou, Zheng

doi:10.1091/mbc.e10-09-0756

Cited by 53 publications

(116 citation statements)

References 71 publications

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“…Snx9 has been implicated in endocytosis, macropinocytosis, phagocytosis (particularly of apoptotic cells), and mitosis (18)(19)(20)(21). The enrichment of PI(4,5)P 2 at the plasma membrane clearly highlights the importance of that location for the Snx9 pathway, and PI(3)P is known to be produced on macropinosomes, phagosomes, and endosomes (22)(23)(24).…”

Section: Discussionmentioning

confidence: 99%

Phosphoinositides and membrane curvature switch the mode of actin polymerization via selective recruitment of toca-1 and Snx9

Gallop

Walrant

Cantley

et al. 2013

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

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The membrane-cytosol interface is the major locus of control of actin polymerization. At this interface, phosphoinositides act as second messengers to recruit membrane-binding proteins. We show that curved membranes, but not flat ones, can use phosphatidylinositol 3-phosphate [PI(3)P] along with phosphatidylinositol 4,5-bisphosphate [PI(4,5)P 2 ] to stimulate actin polymerization. In this case, actin polymerization requires the small GTPase cell cycle division 42 (Cdc42), the nucleation-promoting factor neural Wiskott-Aldrich syndrome protein (N-WASP) and the actin nucleator the actin-related protein (Arp) 2/3 complex. In liposomes containing PI(4,5)P2 as the sole phosphoinositide, actin polymerization requires transducer of Cdc42 activation-1 (toca-1). In the presence of phosphatidylinositol 3-phosphate, polymerization is both more efficient and independent of toca-1. Under these conditions, sorting nexin 9 (Snx9) can be implicated as a specific adaptor that replaces toca-1 to mobilize neural Wiskott-Aldrich syndrome protein and the Arp2/3 complex. This switch in phosphoinositide and adaptor specificity for actin polymerization from membranes has implications for how different types of actin structures are generated at precise times and locations in the cell.T he original discovery of actin as the scaffold in muscle upon which myosin exerts its force obscured for some time that a major role of actin in nonmuscle cells involves its intimate association with cellular membranes. Through morphological studies of the actin cytoskeleton, the close association of actin polymerization and the specification of actin polarity with respect to membranes came to the fore. As the regulatory biochemistry of actin was unraveled, a striking role for regulators with substantial, and regulated, residence in the membrane, such as phosphoinositides and small G proteins, emerged. In the past decades, the extraordinary dynamics of the cytoskeleton as well as the equally extraordinary dynamics of membrane traffic have become centerpieces of cell biological understanding. That an important structural linkage between the dynamics of the membrane and cytoskeleton exists is evident, but how actin regulators are targeted to specific membrane sites is less clear.Phosphoinositides are chemically dynamic lipids that are important upstream regulators of actin assembly (1-3); they can exert their effects through specific protein domains, such as the FYVE (Fab1, YOTB, Vac1, EEA1) domain in EEA1 (early endosome antigen 1) that binds phosphatidylinositol 3-phosphate [PI(3)P]; the pleckstrin homology (PH) domain in Akt that binds phosphatidylinositol (3,4) bisphosphate; and the PH domain in phospholipase Cδ that binds phosphatidylinositol (4,5) bisphosphate [PI(4,5)P 2 ]. The actin polymerization machinery is vast and complex, consisting of nucleators, transducers, cappers, bundlers, and more, many of which are regulated by phosphoinositides (4, 5) and are good candidates to test for biochemical coordination of membrane processes. The fluidity and ...

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Section: Discussionmentioning

confidence: 99%

Phosphoinositides and membrane curvature switch the mode of actin polymerization via selective recruitment of toca-1 and Snx9

Gallop

Walrant

Cantley

et al. 2013

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

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“…Thus, although the SNX3 retromer and SNX-BAR retromer both mediate endosome-to-TGN transport, they constitute distinct, cargo-specific pathways. Indeed, in C. elegans, the retromer-mediated sorting of CED-1 is SNX-BAR-retromer dependent but is independent of the SNX3 retromer (Chen et al 2010;Harterink et al 2011;Lu et al 2011). Furthermore, the morphological profile of each transport carrier is distinct: SNX-BAR retromer residing on nonbranched tubules 170 -230 nm in length and 20 -50 nm in diameter (Mari et al 2008), whereas SNX3 retromer is associated with small clathrin-coated vesicular profiles (Harterink et al 2011).…”

Section: Functionally Distinct Retromer Complexesmentioning

confidence: 99%

Retromer: A Master Conductor of Endosome Sorting

Burd

Cullen

2014

Cold Spring Harbor Perspectives in Biology

395

440

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The endosomal network comprises an interconnected network of membranous compartments whose primary function is to receive, dissociate, and sort cargo that originates from the plasma membrane and the biosynthetic pathway. A major challenge in cell biology is to achieve a thorough molecular description of how this network operates, and in so doing, how defects contribute to the etiology and pathology of human disease. We discuss the increasing body of evidence that implicates an ancient evolutionary conserved complex, termed "retromer," as a master conductor in the complex orchestration of multiple cargo-sorting events within the endosomal network.

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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).…”

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

confidence: 99%

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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Three sorting nexins drive the degradation of apoptotic cells in response to PtdIns(3)P signaling

Cited by 53 publications

References 71 publications

Phosphoinositides and membrane curvature switch the mode of actin polymerization via selective recruitment of toca-1 and Snx9

Phosphoinositides and membrane curvature switch the mode of actin polymerization via selective recruitment of toca-1 and Snx9

Retromer: A Master Conductor of Endosome Sorting

The retromer complex – endosomal protein recycling and beyond

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