Tight Junctions and Cell Polarity

Shin, Kunyoo; Fogg, Vanessa C.; Margolis, Ben

doi:10.1146/annurev.cellbio.22.010305.104219

Cited by 654 publications

(617 citation statements)

References 172 publications

Supporting

Mentioning

612

Contrasting

Unclassified

Order By: Relevance

“…Crumbs and Par cooperate in establishing the apical domain and in the assembly of TJ, whereas Scribble plays a key role in the definition of the basolateral PM domain. They interact with each other through PDZ domains and key phosphorylation events that result in exclusion of Scribble from the apical domain and of Crumbs from the basolateral domain (reviewed by Schock and Perrimon, 2002;Gibson and Perrimon, 2003;Nelson, 2003;Shin et al, 2006;Goldstein and Macara, 2007). aPKC is a key player in the exclusion process, as its phosphorylation of LGL promotes its exclusion from the apical domain and its phosphorylation of Crumbs promotes the localization of this complex to the apical domain (Figure 3a).…”

Section: Domain-identity Machinerymentioning

confidence: 99%

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

2008

View full text Add to dashboard Cite

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.

show abstract

Section: Domain-identity Machinerymentioning

confidence: 99%

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

2008

View full text Add to dashboard Cite

show abstract

“…Here it is noteworthy that the polarity determinants, Drosophila Stardust (Std) and its mammalian orthologue, PALS1/MPP5, are found in septate junctions and TJs, respectively [50]. These are best understood for their roles in determining apical polarity, but it has been known for many years that Std mutants also have defects in AJs [51,52].…”

Section: Tight Junctions and Cadherin Regulation: Cross-talk At The Smentioning

confidence: 99%

Making and breaking contacts: the cellular biology of cadherin regulation

Yap

Crampton

Hardin

2007

Current Opinion in Cell Biology

158

159

View full text Add to dashboard Cite

SummaryCadherin-mediated cell-cell interactions are dynamic processes and cadherin function is tightly regulated in response to cellular context and signaling. Ultimately, cadherin regulation is likely to reflect the interplay between a range of fundamental cellular processes, including surface organization of receptors, cytoskeletal organization and cell trafficking, that are coordinated by signaling events. In this review we focus on recent advances in understanding how interplay with membrane trafficking and other cell-cell junctions can control cadherin function. The endocytosis of cadherins, and their post-internalization fate, influence surface expression and metabolic stability of these adhesion receptors. Similarly, at the surface, components of tight junctions provide a mode of cross-talk that regulates assembly of adherens junctions.

show abstract

“…Recently, mammalian orthologs of two novel, interacting tight junction-associated complexes crucial in establishing and maintaining apico-basal polarity were identified. These evolutionarily conserved protein complexes are known as the Crumbs complex (Crumbs3-PALS1 (protein associated with Lin-7)-PATJ (PALS1-associated tight junction protein)) and the Par complex (Par6-Par3-aPKC (atypical protein kinase C); reviewed by Shin et al, 2006). In mammalian cells, there is strong evidence that the Crumbs and Par complexes control epithelial polarity and apical membrane formation.…”

mentioning

confidence: 99%