Cadherin*:_alpha_-Catenin*:_beta

Complex Cadherin*:_alpha_-Catenin*:_beta_-Catenin*:p120*

Complex composition:

Cadherin*:_alpha_-Catenin*:_beta_-Catenin*:p120*@Cytosol

Identifiers
NAME:Cadherin*:_alpha_-Catenin*:_beta_-Catenin*:p120*

Maps_Modules
HMC:ACTIVATING_INVASION_AND_METASTASIS
EMT Senescence / EMT_REGULATORS
EMT Senescence / CELL_CELL_ADHESIONS
EMT Senescence / ADHERENS_JUNCTIONS

References
PMID:15609097
CTNNB1 (beta-catenin) binds with high affinity to the distal Cadherin cytoplasmic tail.
Cadherin recruits CTNNA1 (alpha-catenin) to the complex.
CTNNA1 (alpha-catenin) binds to Actin filaments directly
CTNNA1 (alpha-catenin) and can also associate with other actin-binding proteins (MLLT4 or Formin)
CTNND1 (delta-catenin or p120) binds directly to Cadherin independently of the other catenins.
Catenins/Cadherin complex can further interact with a range of singaling molecules which participate in either cellular signaling or control of cytoskeletal dynamics.
Stability of Cadherin/Catenins complex and thereby the integrity of adherens junctions is controlled by phosphorylation/dephosphorylation.
PMID:16099633
Phosphorylation of beta-catenin (CTNNB1) by receptor and no-receptor tyrosine kinases results in dissociation of CTNNA1 from CTNNB1 with concomitant loss of cadherin adhesion.
Dephosphoryaltion of CTNNB1 by tyrosine phosphatases ensure or restore the integrity of Cadherin-mediated adhesions.
PMID??:10402472
We conclude that a pool of surface E-cadherin is constantly trafficked through an endocytic, recycling pathway and that this may provide a mechanism for regulating the availability of E-cadherin for junction formation in development, tissue remodeling, and tumorigenesis.
PMID:22674073
Cadherin internalization can occur through either clathrin-mediated, caveolin-mediated, or macropinocytosis-like pathways. Internalized cadherin is then sorted either for lysosomal degradation or recycling back to the plasma membrane.
em_emtc_emtc_re1632( EMT Senescence ):
PMID:16371504
N-cadherin is phosphorylated by c-Src at Tyr-820, Tyr-853, Tyr-860, Tyr-884, and Tyr-886.
Phosphorylation of Tyr-860 (Tyr-835 in E-cadherin) can disrupt cadherin binding to beta-catenin
em_re1454( EMT Senescence ):
Clathrin-mediated endocytosis appears to be responsible for two types of growth factor-induced cadherin internalization, FGF-mediated internalization of E-cadherin () and VEGF-mediated internalization of VE-cadherin.
em_re1484( EMT Senescence ):
Studies have suggested that cadherin endocytosis may occur through both caveolin-mediated and macropinocytosis-like pathways. Akhtar and colleagues found that a dominant-active form of the small GTPase Rac1 could disrupt cell-cell adhesion in keratinocytes. This was associated with the endocytosis of E-cadherin through a pathway that appeared to be distinct from the uptake of transferrin, which is clathrin-mediated, and through structures that co-localized with caveolin
Akhtar and colleagues found that a dominant-active form of the small GTPase Rac1 could disrupt cell-cell adhesion in keratinocytes. This was associated with the endocytosis of E-cadherin through a pathway that appeared to be distinct from the uptake of transferrin, which is clathrin-mediated, and through structures that co-localized with caveolin
In contrast, Bryant and colleagues characterized the EGF-induced internalization of E-cadherin in a breast carcinoma cell line, in which E-cadherin was internalized along with the cadherin-binding proteins p120 and ??-catenin, as Rac1-modulated macropinocytosis
em_re1504( EMT Senescence ):
Desclozeaux and colleagues also found that cadherin recycling is necessary for maintaining adherens junctions.

Modifications:
Participates in complexes:
In compartment: Cytosol

Cadherin*:_alpha_-Catenin*:_beta_-Catenin*:p120*@Cytosol

Participates in reactions:
As Reactant or Product:

As Catalyser: