2005
DOI: 10.1016/j.yexcr.2005.04.017
|View full text |Cite
|
Sign up to set email alerts
|

Layilin, a cell surface hyaluronan receptor, interacts with merlin and radixin

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
2
2
1

Citation Types

0
35
0
1

Year Published

2008
2008
2024
2024

Publication Types

Select...
6
1

Relationship

0
7

Authors

Journals

citations
Cited by 54 publications
(38 citation statements)
references
References 60 publications
(68 reference statements)
0
35
0
1
Order By: Relevance
“…We confirmed that layilin specifically binds HA (39) as reported previously. What pointed toward layilin as an ideal HA receptor to be involved epithelial permeability is that it is known to interact with members of the ezrin, radixin, and moesin proteins (81) that are key regulators of cytoskeletonplasma membrane interactions in polarized cell. CD44 and RHAMM are two of the better characterized HA receptors in airway epithelial cells (19,21,(82)(83)(84), but in intact epithelium CD44 expression is restricted to the basolateral domain (83,85,86) and thus, at least initially, cannot be accessed by fragments released during luminal HA degradation.…”
Section: Discussionmentioning
confidence: 99%
“…We confirmed that layilin specifically binds HA (39) as reported previously. What pointed toward layilin as an ideal HA receptor to be involved epithelial permeability is that it is known to interact with members of the ezrin, radixin, and moesin proteins (81) that are key regulators of cytoskeletonplasma membrane interactions in polarized cell. CD44 and RHAMM are two of the better characterized HA receptors in airway epithelial cells (19,21,(82)(83)(84), but in intact epithelium CD44 expression is restricted to the basolateral domain (83,85,86) and thus, at least initially, cannot be accessed by fragments released during luminal HA degradation.…”
Section: Discussionmentioning
confidence: 99%
“…2,3 Layilin is a widely expressed 55-kDa type 1 transmembrane protein that contains an extracellular domain homologous with the carbohydrate-recognition domain of C-type lectins. 4 The homology between layilin and selectins, which are involved in the initial adhesion of lymphocytes to endothelial cells, has led to the suggestion that layilin supports transient adhesion, which allows the subsequent assembly of more stable, although still short-lived, focal complexes (FXs). 4,5 Adhesion in FXs is mediated by the wellcharacterised integrin family of dimeric receptors 6 that bind to proteins rather than the carbohydrate components of the ECM.…”
Section: Introductionmentioning
confidence: 99%
“…4 The homology between layilin and selectins, which are involved in the initial adhesion of lymphocytes to endothelial cells, has led to the suggestion that layilin supports transient adhesion, which allows the subsequent assembly of more stable, although still short-lived, focal complexes (FXs). 4,5 Adhesion in FXs is mediated by the wellcharacterised integrin family of dimeric receptors 6 that bind to proteins rather than the carbohydrate components of the ECM. Some FXs transform into larger, more stable structures called focal adhesions (FAs) as a result of RhoA-mediated actomyosin contraction 7,8 or exposure to mechanical force.…”
Section: Introductionmentioning
confidence: 99%
“…It is approximately a 55 kDa transmembrane protein that shares structural similarity to C-type lectins [52]. Although the structure of layilin has been found to be different from CD44 receptor [52], they share a common ligand on the extracellular and cytosolic surfaces [52,78]. The affinity of hyaluronan for the extracellular domain of layilin parallels hyaluronan-CD44 complexes [52].…”
Section: Layilinmentioning
confidence: 99%
“…On the cytosolic domain, layilin binds to merlin, radixin, and talin, which are members of the ERM family [52,78]. These interactions have a downstream effect on cell migration and tumor metastasis [52,78].…”
Section: Layilinmentioning
confidence: 99%