Interactions between the discoidin domain receptor 1 and β1 integrin regulate attachment to collagen
Collagen degradation by phagocytosis is essential for physiological collagen turnover and connective tissue homeostasis. The rate limiting step of phagocytosis is the binding of specific adhesion receptors, which include the integrins and discoidin domain receptors (DDR), to fibrillar collagen. Whil...
Main Authors: | Staudinger, Lisa A., Spano, Stephen J., Lee, Wilson, Coelho, Nuno, Rajshankar, Dhaarmini, Bendeck, Michelle P., Moriarty, Tara, McCulloch, Christopher A. |
---|---|
Format: | Online |
Language: | English |
Published: |
The Company of Biologists
2013
|
Online Access: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3828761/ |
Similar Items
-
Collagen recognition and transmembrane signalling by discoidin domain receptors☆
by: Carafoli, Federico, et al.
Published: (2013) -
Discoidin Domain Receptors Promote α1β1- and α2β1-Integrin Mediated Cell Adhesion to Collagen by Enhancing Integrin Activation
by: Xu, Huifang, et al.
Published: (2012) -
Collagen I–mediated up-regulation of N-cadherin requires cooperative signals from integrins and discoidin domain receptor 1
by: Shintani, Yasushi, et al.
Published: (2008) -
ADAM10 controls collagen signaling and cell migration on collagen by shedding the ectodomain of discoidin domain receptor 1 (DDR1)
by: Shitomi, Yasuyuki, et al.
Published: (2015) -
Type I collagen fibrils and discoidin domain receptor 1 set invadosomes straight
by: Moreau, Violaine, et al.
Published: (2015)