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Stimulation‐Dependent Recycling of Integrin β1 Regulated by ARF6 and Rab11
In comparison to the internalization pathways of endocytosis, the recycling pathways are less understood. Even less defined is the process of regulated recycling, as few examples exist and their…
Nesprin-3, a novel outer nuclear membrane protein, associates with the cytoskeletal linker protein plectin
Plectin binds to the integrin α6β4 at the cell surface and to nesprin-3 at the ONM in keratinocytes, suggesting that there is a continuous connection between the nucleus and the extracellular matrix through the IF cytoskeleton.
Recombinant Vitronectin Is a Functionally Defined Substrate That Supports Human Embryonic Stem Cell Self‐Renewal via αVβ5 Integrin
Recombinant vitronectin was the only defined functional alternative to Matrigel, supporting sustained self‐renewal and pluripotency in three independent hESC lines and eliminating the need for defined medium supplements and ECM proteins.
Function and interactions of integrins
An overview is given of the function and ligand-binding properties of integrins as well as of proteins that associate withintegrins and may play a role in their signaling function.
Mouse egg integrin alpha 6 beta 1 functions as a sperm receptor.
A novel role for the integrin alpha 6 beta 1 as a cell-cell adhesion receptor that mediates sperm-egg binding is indicated, as well as a function-blocking anti-alpha v beta 3 polyclonal antibody.
Mechanisms of integrin activation and trafficking.
Structure and function of hemidesmosomes: more than simple adhesion complexes.
The aims of this review are to highlight the recent progresses of knowledge on the organization and assembly of hemidesmosomes, their involvement in signaling pathways as well as their participation in clinical pathologic conditions.
Vinculin potentiates E-cadherin mechanosensing and is recruited to actin-anchored sites within adherens junctions in a myosin II–dependent manner
Vinculin localizes to tension-bearing cell–cell junctions to help transmit signals from E-cadherin to the actin cytoskeleton in response to mechanical stress.
Current insights into the formation and breakdown of hemidesmosomes.
The Tetraspan Molecule Cd151, a Novel Constituent of Hemidesmosomes, Associates with the Integrin α6β4 and May Regulate the Spatial Organization of Hemidesmosomes
- L. Sterk, C. Geuijen, L. Oomen, J. Calafat, H. Janssen, A. Sonnenberg
- BiologyThe Journal of cell biology
- 15 May 2000
It is demonstrated that in human skin CD151 is codistributed with α3β1 and α6β4 at the basolateral surface of basal keratinocytes, and it is suggested that CD151 plays a role in the formation and stability of hemidesmosomes by providing a framework for the spatial organization of the differenthemidesmosomal components.