The intracellular lumen: origin, role and implications of a cytoplasmic neostructure

Rémy, Lionel

doi:10.1111/j.1768-322x.1986.tb00446.x

Cited by 49 publications

(29 citation statements)

References 0 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…A similar phenotype is observed in Rab8-knockout mice (Sato et al, 2007), and previous work has shown evidence of interactions between Rab8 and myosin-Vb (Roland et al, 2007). Intracellular vacuoles, also called intracellular lumens (Remy, 1986) or VACs (vacuolar apical compartments) (Vega-Salas et al, 1988), are often observed in transformed epithelial cells and in epithelial cells deprived of cell-cell contacts. They are thought to be normal intermediates in the biogenesis of the apical surface in epithelial and endothelial cells, and often result from the fusion of apical-transport vesicles under conditions of reduced delivery to the apical PM (Verges et al, 2007).…”

Section: Rho Gtpases and Actin Dynamics In Apical Deliverymentioning

confidence: 56%

Apical trafficking in epithelial cells: signals, clusters and motors

Weisz

Rodríguez-Boulan

2009

Journal of Cell Science

284

285

View full text Add to dashboard Cite

In the early days of epithelial cell biology, researchers working with kidney and/or intestinal epithelial cell lines and with hepatocytes described the biosynthetic and recycling routes followed by apical and basolateral plasma membrane (PM) proteins. They identified the trans-Golgi network and recycling endosomes as the compartments that carried out apical-basolateral sorting. They described complex apical sorting signals that promoted association with lipid rafts, and simpler basolateral sorting signals resembling clathrin-coated-pit endocytic motifs. They also noticed that different epithelial cell types routed their apical PM proteins very differently, using either a vectorial (direct) route or a transcytotic (indirect) route. Although these original observations have generally held up, recent studies have revealed interesting complexities in the routes taken by apically destined proteins and have extended our understanding of the machinery required to sustain these elaborate sorting pathways. Here, we critically review the current status of apical trafficking mechanisms and discuss a model in which clustering is required to recruit apical trafficking machineries. Uncovering the mechanisms responsible for polarized trafficking and their epithelial-specific variations will help understand how epithelial functional diversity is generated and the pathogenesis of many human diseases.

show abstract

Section: Rho Gtpases and Actin Dynamics In Apical Deliverymentioning

confidence: 56%

Apical trafficking in epithelial cells: signals, clusters and motors

Weisz

Rodríguez-Boulan

2009

Journal of Cell Science

284

285

View full text Add to dashboard Cite

show abstract

Section: Sustained Inhibition Of Epithelial Polarity Causes Intracellmentioning

confidence: 91%

“…This compartment was termed "vacuolar apical compartment" or VAC (Vega-Salas et al, 1987). Similar vacuoles are found in a variety of carcinomas (Remy, 1986;Kern et al, 1987; VegaSalas et al, 1993).We studied the subcellular localization of plasma membrane SNAREs in MDCK cells grown under these conditions. A high percentage (Ͼ50%) of the cells display one or more large vacuolar compartments that are positive for the endogenous apical marker protein gp135 and are indistinguishable in appearance from previously described VACs (Figure 4).…”

mentioning

confidence: 87%

“…First, VACs have been observed by others in mammary carcinoma cells grown in medium containing a regular calcium concentration . Second, VAC-like organelles are frequently found in a variety of carcinomas in situ (Remy, 1986;Vega-Salas et al, 1993) and in intestinal epithelial cells in the genetic disorder microvillus inclusion disease (Ameen and Salas, 2000). Third, the intracellular calcium concentration has been measured previously in MDCK cells grown in high-or low-calcium medium and was found to be not significantly different (VegaSalas et al, 1987).…”

Section: Sh Low Et Almentioning

confidence: 97%

See 1 more Smart Citation

Intracellular Redirection of Plasma Membrane Trafficking after Loss of Epithelial Cell Polarity

Low

Miura²,

Roche

et al. 2000

MBoC

View full text Add to dashboard Cite

In polarized Madin-Darby canine kidney epithelial cells, components of the plasma membrane fusion machinery, the t-SNAREs syntaxin 2, 3, and 4 and SNAP-23, are differentially localized at the apical and/or basolateral plasma membrane domains. Here we identify syntaxin 11 as a novel apical and basolateral plasma membrane t-SNARE. Surprisingly, all of these t-SNAREs redistribute to intracellular locations when Madin-Darby canine kidney cells lose their cellular polarity. Apical SNAREs relocalize to the previously characterized vacuolar apical compartment, whereas basolateral SNAREs redistribute to a novel organelle that appears to be the basolateral equivalent of the vacuolar apical compartment. Both intracellular plasma membrane compartments have an associated prominent actin cytoskeleton and receive membrane traffic from cognate apical or basolateral pathways, respectively. These findings demonstrate a fundamental shift in plasma membrane traffic toward intracellular compartments while protein sorting is preserved when epithelial cells lose their cell polarity. INTRODUCTIONTraffic between membranous compartments is mediated by the soluble N-ethylmaleimide-sensitive factor attachment protein (SNARE) machinery in virtually all membrane traffic pathways investigated so far (Rothman and Warren, 1994;Hanson et al., 1997;Hay and Scheller, 1997;Nichols and Pelham, 1998). During vesicle docking, membrane proteins on the vesicle membrane (v-SNAREs) and the target membrane (t-SNAREs) bind to each other to form a complex that ultimately leads to fusion of the lipid bilayers. One aspect of the SNARE hypothesis is that successful membrane fusion requires the binding of matching combinations of v-and t-SNAREs, thereby ensuring the necessary specificity of vesicle fusion. Accordingly, each membrane organelle and each class of transport vesicles should be defined by a certain set of t-and v-SNARE isoforms. Many SNAREs have been identified to date, and protein sequence analysis has shown that v-and t-SNAREs of the currently known SNARE subfamilies are evolutionarily related to each other and belong to a common superfamily (Weimbs et al., 1997b(Weimbs et al., , 1998. It is conceivable that the specificity of vesicle fusion is not directly determined by t-SNARE/v-SNARE interactions per se but rather by interactions involving larger complexes, including SNAREs and their regulatory proteins, such as those of the rab and sec1 protein families (Christoforidis et al., 1999;Gonzalez and Scheller, 1999;Pfeffer, 1999).Epithelial cells display an additional layer of complexity in that they are typically polarized and possess two distinct plasma membrane domains (Louvard et al., 1992;Simons et al., 1992;Le Gall et al., 1995;Drubin and Nelson, 1996;Yeaman et al., 1999). The apical and basolateral plasma membrane domains have different protein and lipid compositions that reflect the different functions of these domains. This plasma membrane polarity is established and maintained by protein sorting and specific vesicle trafficking routes in th...

show abstract

“…This compartment was termed 'vacuolar apical compartment' or VAC (38). Similar vacuoles are found in a variety of carcinomas (16,31,40).…”

Section: Bodymentioning

confidence: 93%

Effects of c-Myc and TGF-Alpha on Polarized Membrane Traffic

Altschuler¹,

Mostov²

2000

View full text Add to dashboard Cite

1 069u r REPORT DOCUMENTATION PAGE I 0MBNo. Public reporting burde~nfor this collection of information is estimated to average 1 hour per response, including the time for reviewing instructions, searching existing data sources, gathering and maintaining the data needed, and completing and reviewing this collection of information. Send comments regarding this burden estimate or any other aspect of this collection of information, including suggestions for reducing this burden to Washington Headquarters Services, Directorate for Information Operations and Reports, 1215 Jefferson Davis Highway, Suite 1204, Arlington, VA 22202-4302, and to the Office of Management and Budget, Paperwork Reduction Project (0704-0188), Washington, DC 20503

show abstract

The intracellular lumen: origin, role and implications of a cytoplasmic neostructure

Cited by 49 publications

References 0 publications

Apical trafficking in epithelial cells: signals, clusters and motors

Apical trafficking in epithelial cells: signals, clusters and motors

Intracellular Redirection of Plasma Membrane Trafficking after Loss of Epithelial Cell Polarity

Effects of c-Myc and TGF-Alpha on Polarized Membrane Traffic

Contact Info

Product

Resources

About