Organization of vesicular trafficking in epithelia

Rodríguez-Boulan, Enrique; Kreitzer, Geri; Müsch, Anne

doi:10.1038/nrm1593

Cited by 570 publications

(591 citation statements)

References 159 publications

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“…Apical and basolateral PM proteins are synthesized at the endoplasmic reticulum, transported to the Golgi complex and sorted at the trans golgi network (TGN) into distinct apical and basolateral vesicular routes (Simons and Wandinger-Ness, 1990;Rodriguez-Boulan and Powell, 1992). After arrival at the cell surface, apical and basolateral membrane proteins are internalized into separate apical sorting endosomes and basal sorting endosomes (Figure 2), (Breitfeld et al, 1989;Mostov et al, 2003;Rodriguez-Boulan et al, 2005), mixed in common recycling endosomes and sorted into distinct recycling routes back to their original PM domain. The apical recycling route includes the apical recycling endosome (Apodaca et al, 1994;Brown et al, 2000).…”

Section: Polarized Trafficking Machinerymentioning

confidence: 99%

“…Basolateral sorting is guided by basolateral sorting signals (Keller and Simons, 1997;Rodriguez-Boulan et al, 2005), and they include: short tyrosine motifs such as Yxxf or NPXY (Brewer and Roth, 1991;Le Bivic et al, 1991;Matter et al, 1992), dileucine (Hunziker and Fumey, 1994) or monoleucine motifs with nearby acidic patches (Deora et al, 2004), PxxP, found in EGFR and pleomorphic motifs that do not yet fall into established classes, found in NCAM (Le Gall et al, 1994), transferrin receptor (Odorizzi and Trowbridge, 1997) and polymeric IgA receptor (Aroeti and Mostov, 1994) ( Figure 2). Yeast 2 and 3 hybrid assays (Ohno et al, 1995;Janvier et al, 2003) demonstrated that Yxxf motifs interact with the m subunit of AP adaptors (AP1, AP2, AP3, AP4), whereas dileucine motifs of the type [DE]XXXL [LI] bind to g and s1 subunits of AP1 and to d and s3 subunits of AP3 (Kirchhausen, 2000;Bonifacino and Traub, 2003).…”

Section: Polarized Trafficking Machinerymentioning

confidence: 99%

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The epithelial polarity program: machineries involved and their hijacking by cancer

2008

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The Epithelial Polarity Program (EPP) adapts and integrates three ancient cellular machineries to construct an epithelial cell. The polarized trafficking machinery adapts the cytoskeleton and ancestral secretory and endocytic machineries to the task of sorting and delivering different plasma membrane (PM) proteins to apical and basolateral surface domains. The domain-identity machinery builds a tight junctional fence (TJ) between apical and basolateral PM domains and adapts ancient polarity proteins and polarity lipids on the cytoplasmic side of the PM, which have evolved to perform a diversity of polarity tasks across cells and species, to provide 'identity' to each epithelial PM domain. The 3D organization machinery utilizes adhesion molecules as positional sensors of other epithelial cells and the basement membrane and small GTPases as integrators of positional information with the activities of the domain-identity and polarized trafficking machineries. Cancer is a disease mainly of epithelial cells (90% of human cancers are carcinomas that derive from epithelial cells) that hijacks the EPP machineries, resulting in loss of epithelial polarity, which often correlates in extent with the aggressiveness of the tumor. Here, we review how the EPP integrates its three machineries and the strategies used by cancer to hijack them.

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Section: Polarized Trafficking Machinerymentioning

confidence: 99%

Section: Polarized Trafficking Machinerymentioning

confidence: 99%

The epithelial polarity program: machineries involved and their hijacking by cancer

2008

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“…This is 171 based on highly specific sorting machinery at the exit of the 172 TGN (Rodriguez-Boulan et al 2005). Cytoskeleton ele-173 ments form part of this machinery, and the integrity of 174 actin filaments is necessary for efficient delivery of some 175 proteins destined for the apical or the basolateral plasma 176 membrane domains in both polarized and non-polarized 177 cells, but not for the transport of lipid raft-associated pro-178 teins (Jacob et al 2003;Lazaro-Dieguez et al 2007;179 Lebreton et al 2008) (Fig.…”

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confidence: 99%

Actin acting at the Golgi

Egea

Serra‐Peinado

Salcedo-Sicilia

et al. 2013

Histochem Cell Biol

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7 Abstract The organization, assembly and remodeling of 8 the actin cytoskeleton provide force and tracks for a variety 9 of (endo)membrane-associated events such as membrane 10 trafficking. This review illustrates in different cellular 11 models how actin and many of its numerous binding and 12 regulatory proteins (actin and co-workers) participate in the 13 structural organization of the Golgi apparatus and in traf-14 ficking-associated processes such as sorting, biogenesis and 15 motion of Golgi-derived transport carriers. 16 17 Keywords Golgi apparatus Á Cytoskeleton Á Actin Á 18 Spectrin Á Myosin Á Rho GTPases Introduction 20The function of the Golgi apparatus is the result of a 21 complex interaction between the molecules that establish 22 its architecture, those that determine protein transport and 23 those that integrate signals from either outside or inside the 24 cell. Cytoskeletal elements (microtubules, actin filaments 25 or microfilaments and intermediate filaments) integrate 26 these processes. Association and coordination between 27 them as well as their respective binding and regulatory 28 proteins are present in the majority of endomembrane 29 systems, including the Golgi apparatus. While its basic 30 function is highly conserved, the Golgi varies greatly in 31 shape and number from one organism to another. Briefly, it 32 ranges from dispersed cisternae or isolated tubular net-33 works as occurs in algae, protozoa and the yeast Saccha-34 romyces cerevisiae, to a pile of flattened cisternae aligned 35 in parallel and known as the Golgi stack. This, depending 36 on the organism examined, could be present in a single 37 (fungi and the yeast Pichia pastoris) or multiple copies, the 38 latter being scattered throughout the cytoplasm (plants and 39 Drosophila) or organized as a ribbon around centrioles 40 (vertebrates) (daSilva et al. 2004; Hawes and Satiat-Je-41 unemaitre 2005; He et al. 2004;He2007; Henderson et al. 42 2007; Kondylis and Rabouille 2003; Ladinsky et al. 1999; 43 Lowe 2011; Mogelsvang et al. 2003; Pelletier et al. 2002; 44 Preuss et al. 1992;Rambourg and Clermont 1986; Ram-45 bourg et al. 2001;Ramírez and Lowe 2009; Rios and 46 Bornens 2003; Rossanese et al. 1999). The cytoskeleton 47 determines the location of the Golgi, and depending on the 48 cellular model, either microtubules or actin filaments have 49 the greater influence (Egea and Rios 2008), the impact of 50 intermediate filaments being very limited (Gao and Sztul 51 2001; Gao et al. 2002;Styers et al. 2006; Toivola et al. 52 2005). Historically, microtubules were the first cytoskele-53 ton element to be linked to the Golgi structure and function 54 (Thyberg and Moskalewski 1999), and only later was it 55 firmly established that actin and associated proteins (actin 56 et al.) also played a significant role (for recent reviews see 44Histochem Cell Biol DOI 10.1007/s00418-013-1115 Author Proof U N C O R R E C T E D P R O O F63 between the actin-based cytoskeleton and the Golgi in a 64 variety of cellular models ...

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“…During embryonic and postnatal development, these transport events are tightly coordinated with the activities of other cellular systems (e.g., the cytoskeleton, adhesion patches) through numerous signaling proteins (Nelson, 2003;Rodriguez-Boulan et al, 2005). Mutations in these regulatory proteins can therefore induce genetic disorders that are frequently accompanied by severe phenotypes.…”

Section: Introductionmentioning

confidence: 99%

“…Membrane transport has a fundamental role in tissue biogenesis through its supply of extracellular matrix components, surface adhesion molecules, and the lipids and proteins that are essential for specific cell-surface domains (Mostov et al, 2003;Nelson, 2003;Rodriguez-Boulan et al, 2005). During embryonic and postnatal development, these transport events are tightly coordinated with the activities of other cellular systems (e.g., the cytoskeleton, adhesion patches) through numerous signaling proteins (Nelson, 2003;Rodriguez-Boulan et al, 2005).…”

Section: Introductionmentioning

confidence: 99%

Faciogenital Dysplasia Protein (FGD1) Regulates Export of Cargo Proteins from the Golgi Complex via Cdc42 Activation

Egorov

Capestrano

Vorontsova

et al. 2009

MBoC

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Mutations in the FGD1 gene are responsible for the X-linked disorder known as faciogenital dysplasia (FGDY). FGD1 encodes a guanine nucleotide exchange factor that specifically activates the GTPase Cdc42. In turn, Cdc42 is an important regulator of membrane trafficking, although little is known about FGD1 involvement in this process. During development, FGD1 is highly expressed during bone growth and mineralization, and therefore a lack of the functional protein leads to a severe phenotype. Whether the secretion of proteins, which is a process essential for bone formation, is altered by mutations in FGD1 is of great interest. We initially show here that FGD1 is preferentially associated with the trans-Golgi network (TGN), suggesting its involvement in export of proteins from the Golgi. Indeed, expression of a dominant-negative FGD1 mutant and RNA interference of FGD1 both resulted in a reduction in post-Golgi transport of various cargoes (including bone-specific proteins in osteoblasts). Live-cell imaging reveals that formation of post-Golgi transport intermediates directed to the cell surface is inhibited in FGD1-deficient cells, apparently due to an impairment of TGN membrane extension along microtubules. These effects depend on FGD1 regulation of Cdc42 activation and its association with the Golgi membranes, and they may contribute to FGDY pathogenesis.

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Organization of vesicular trafficking in epithelia

Cited by 570 publications

References 159 publications

The epithelial polarity program: machineries involved and their hijacking by cancer

The epithelial polarity program: machineries involved and their hijacking by cancer

Actin acting at the Golgi

Faciogenital Dysplasia Protein (FGD1) Regulates Export of Cargo Proteins from the Golgi Complex via Cdc42 Activation

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