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Gene Review:

VEZT - vezatin, adherens junctions transmembrane...

Homo sapiens

Synonyms: DKFZP761C241, Vezatin

Küssel-Andermann, P. et al., Sousa, S. et al., Blaschuk, O.W. et al.

Blaschuk, Rowlands,

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Disease relevance of VEZT

Here, we demonstrate by pharmacological and genetic approaches that both myosin VIIa and vezatin are crucial for Listeria internalization [1].

High impact information on VEZT

In myosin VIIA-defective mutants, inactivity of the vezatin-myosin VIIA complex at both sites could account for splaying out of the hair cell stereocilia [2].
In the inner ear sensory hair cells vezatin is, in addition, concentrated at another membrane-membrane interaction site, namely at the fibrillar links interconnecting the bases of adjacent stereocilia [2].
We have recently identified an unconventional myosin, myosin VIIa and its ligand vezatin, at the adherens junctions of polarized epithelial cells [1].
This review focuses on the three known plasma membrane components of adherens junctions: E-cadherin, nectin-2 and vezatin [3].

Anatomical context of VEZT

Unconventional myosin VIIa and vezatin, two proteins crucial for Listeria entry into epithelial cells [1].

Other interactions of VEZT

Vezatin, a novel transmembrane protein, bridges myosin VIIA to the cadherin-catenins complex [2].

References

Unconventional myosin VIIa and vezatin, two proteins crucial for Listeria entry into epithelial cells. Sousa, S., Cabanes, D., El-Amraoui, A., Petit, C., Lecuit, M., Cossart, P. J. Cell. Sci. (2004) [Pubmed]
Vezatin, a novel transmembrane protein, bridges myosin VIIA to the cadherin-catenins complex. Küssel-Andermann, P., El-Amraoui, A., Safieddine, S., Nouaille, S., Perfettini, I., Lecuit, M., Cossart, P., Wolfrum, U., Petit, C. EMBO J. (2000) [Pubmed]
Plasma membrane components of adherens junctions (Review). Blaschuk, O.W., Rowlands, T.M. Mol. Membr. Biol. (2002) [Pubmed]

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vezt	Xenopus (Silurana) tropicalis

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