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  1. Article ; Online: Regulation of cadherin trafficking.

    Delva, Emmanuella / Kowalczyk, Andrew P

    Traffic (Copenhagen, Denmark)

    2008  Volume 10, Issue 3, Page(s) 259–267

    Abstract: ... trafficking by catenins and the interplay between growth factor signaling pathways and cadherin endocytosis. ... cadherins are routed and how the interface between cadherins and membrane trafficking pathways regulates ... cell surface adhesive potential. Particular emphasis is placed on the regulation of cadherin ...

    Abstract Cadherins are a large family of cell-cell adhesion molecules that tether cytoskeletal networks of actin and intermediate filaments to the plasma membrane. This function of cadherins promotes tissue organization and integrity, as demonstrated by numerous disease states that are characterized by the loss of cadherin-based adhesion. However, plasticity in cell adhesion is often required in cellular processes such as tissue patterning during development and epithelial migration during wound healing. Recent work has revealed a pivotal role for various membrane trafficking pathways in regulating cellular transitions between quiescent adhesive states and more dynamic phenotypes. The regulation of cadherins by membrane trafficking is emerging as a key player in this balancing act, and studies are beginning to reveal how this process goes awry in the context of disease. This review summarizes the current understanding of how cadherins are routed and how the interface between cadherins and membrane trafficking pathways regulates cell surface adhesive potential. Particular emphasis is placed on the regulation of cadherin trafficking by catenins and the interplay between growth factor signaling pathways and cadherin endocytosis.
    MeSH term(s) Animals ; Cadherins/chemistry ; Cadherins/metabolism ; Catenins/metabolism ; Disease ; Endocytosis ; Humans ; Intercellular Signaling Peptides and Proteins/metabolism ; Protein Transport
    Chemical Substances Cadherins ; Catenins ; Intercellular Signaling Peptides and Proteins
    Language English
    Publishing date 2008-12-04
    Publishing country England
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Review
    ZDB-ID 1483852-7
    ISSN 1600-0854 ; 1398-9219
    ISSN (online) 1600-0854
    ISSN 1398-9219
    DOI 10.1111/j.1600-0854.2008.00862.x
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  2. Article: Regulation of Cadherin Trafficking

    Delva, Emmanuella / Kowalczyk, Andrew P

    Traffic. 2009 Mar., v. 10, no. 3

    2009  

    Abstract: ... trafficking by catenins and the interplay between growth factor signaling pathways and cadherin endocytosis. ... cadherins are routed and how the interface between cadherins and membrane trafficking pathways regulates ... cell surface adhesive potential. Particular emphasis is placed on the regulation of cadherin ...

    Abstract Cadherins are a large family of cell-cell adhesion molecules that tether cytoskeletal networks of actin and intermediate filaments to the plasma membrane. This function of cadherins promotes tissue organization and integrity, as demonstrated by numerous disease states that are characterized by the loss of cadherin-based adhesion. However, plasticity in cell adhesion is often required in cellular processes such as tissue patterning during development and epithelial migration during wound healing. Recent work has revealed a pivotal role for various membrane trafficking pathways in regulating cellular transitions between quiescent adhesive states and more dynamic phenotypes. The regulation of cadherins by membrane trafficking is emerging as a key player in this balancing act, and studies are beginning to reveal how this process goes awry in the context of disease. This review summarizes the current understanding of how cadherins are routed and how the interface between cadherins and membrane trafficking pathways regulates cell surface adhesive potential. Particular emphasis is placed on the regulation of cadherin trafficking by catenins and the interplay between growth factor signaling pathways and cadherin endocytosis.
    Keywords desmosomes ; endocytosis ; growth factors
    Language English
    Dates of publication 2009-03
    Size p. 259-267.
    Publisher Blackwell Publishing Ltd
    Publishing place Oxford, UK
    Document type Article
    ZDB-ID 1483852-7
    ISSN 1600-0854 ; 1398-9219
    ISSN (online) 1600-0854
    ISSN 1398-9219
    DOI 10.1111/j.1600-0854.2008.00862.x
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  3. Article ; Online: Cadherin tales: Regulation of cadherin function by endocytic membrane trafficking.

    Cadwell, Chantel M / Su, Wenji / Kowalczyk, Andrew P

    Traffic (Copenhagen, Denmark)

    2016  Volume 17, Issue 12, Page(s) 1262–1271

    Abstract: ... of cadherin membrane trafficking. ... membrane trafficking has emerged as a fundamental mechanism by which cells confer a dynamic state ... multiple endocytic motifs, or "switches," that can be used by cellular membrane trafficking machinery ...

    Abstract Cadherins are the primary adhesion molecules in adherens junctions and desmosomes and play essential roles in embryonic development. Although significant progress has been made in understanding cadherin structure and function, we lack a clear vision of how cells confer plasticity upon adhesive junctions to allow for cellular rearrangements during development, wound healing and metastasis. Endocytic membrane trafficking has emerged as a fundamental mechanism by which cells confer a dynamic state to adhesive junctions. Recent studies indicate that the juxtamembrane domain of classical cadherins contains multiple endocytic motifs, or "switches," that can be used by cellular membrane trafficking machinery to regulate adhesion. The cadherin-binding protein p120-catenin (p120) appears to be the master regulator of access to these switches, thereby controlling cadherin endocytosis and turnover. This review focuses on p120 and other cadherin-binding proteins, ubiquitin ligases, and growth factors as key modulators of cadherin membrane trafficking.
    MeSH term(s) Adherens Junctions/metabolism ; Adherens Junctions/physiology ; Animals ; Cadherins/metabolism ; Cell Adhesion/physiology ; Cell Membrane/metabolism ; Cell Membrane/physiology ; Embryonic Development/physiology ; Endocytosis/physiology ; Humans ; Protein Transport
    Chemical Substances Cadherins
    Language English
    Publishing date 2016-12
    Publishing country England
    Document type Journal Article ; Review
    ZDB-ID 1483852-7
    ISSN 1600-0854 ; 1398-9219
    ISSN (online) 1600-0854
    ISSN 1398-9219
    DOI 10.1111/tra.12448
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  4. Article: Regulation of AMPA receptor trafficking by N-cadherin.

    Nuriya, Mutsuo / Huganir, Richard L

    Journal of neurochemistry

    2006  Volume 97, Issue 3, Page(s) 652–661

    Abstract: ... cadherin was found to associate with AMPA receptors and regulate AMPA receptor trafficking in neurons. N ... AMPA) receptor trafficking. Although these two forms of plasticity appear to be highly coordinated ... cadherin and beta-catenin formed a protein complex with AMPA receptors in vivo, and this association was ...

    Abstract Dendritic spines are dynamically regulated, both morphologically and functionally, by neuronal activity. Morphological changes are mediated by a variety of synaptic proteins, whereas functional changes can be dramatically modulated by the regulation of alpha-amino-3-hydroxy-5-methylisoxazole-4-propionate (AMPA) receptor trafficking. Although these two forms of plasticity appear to be highly coordinated, the connections between them are not fully understood. In this study the synaptic cell adhesion molecule N-cadherin was found to associate with AMPA receptors and regulate AMPA receptor trafficking in neurons. N-cadherin and beta-catenin formed a protein complex with AMPA receptors in vivo, and this association was regulated by extracellular Ca2+. In addition, these proteins co-clustered at synapses in cultured neurons. In heterologous cells and in cultured neurons, overexpression of wild-type N-cadherin specifically increased the surface expression level of the AMPA receptor subunit glutamate receptor 1 (GluR1) and this effect was reversed by a dominant-negative form of N-cadherin. Finally, GluR1 increased the surface expression of N-cadherin in heterologous cells. Importantly, recent studies suggest that N-cadherin and beta-catenin play key roles in structural plasticity in neurons. Therefore, our data suggest that the association of N-cadherin with AMPA receptors may serve as a biochemical link between structural and functional plasticity of synapses.
    MeSH term(s) Animals ; Animals, Newborn ; Brain/cytology ; Cadherins/genetics ; Cadherins/metabolism ; Calcium/metabolism ; Cells, Cultured ; Embryo, Mammalian ; Green Fluorescent Proteins/metabolism ; Humans ; Immunohistochemistry/methods ; Immunoprecipitation/methods ; Mice ; Mutagenesis/physiology ; Neurons/cytology ; Neurons/physiology ; Protein Transport/physiology ; Rats ; Rats, Sprague-Dawley ; Receptors, AMPA/classification ; Receptors, AMPA/metabolism ; Transfection/methods ; beta Catenin/metabolism
    Chemical Substances Cadherins ; Receptors, AMPA ; beta Catenin ; Green Fluorescent Proteins (147336-22-9) ; Calcium (SY7Q814VUP)
    Language English
    Publishing date 2006-05
    Publishing country England
    Document type Comparative Study ; Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 80158-6
    ISSN 1471-4159 ; 0022-3042 ; 1474-1644
    ISSN (online) 1471-4159
    ISSN 0022-3042 ; 1474-1644
    DOI 10.1111/j.1471-4159.2006.03740.x
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  5. Article: Regulation of AMPA receptor trafficking by N-cadherin

    Nuriya, Mutsuo / Huganir, Richard L

    Journal of neurochemistry. 2006, v. 97, no. 3

    2006  

    Abstract: ... cadherin was found to associate with AMPA receptors and regulate AMPA receptor trafficking in neurons. N ... receptor trafficking. Although these two forms of plasticity appear to be highly coordinated ... cadherin and β-catenin formed a protein complex with AMPA receptors in vivo, and this association was ...

    Abstract Dendritic spines are dynamically regulated, both morphologically and functionally, by neuronal activity. Morphological changes are mediated by a variety of synaptic proteins, whereas functional changes can be dramatically modulated by the regulation of α-amino-3-hydroxy-5-methylisoxazole-4-propionate (AMPA) receptor trafficking. Although these two forms of plasticity appear to be highly coordinated, the connections between them are not fully understood. In this study the synaptic cell adhesion molecule N-cadherin was found to associate with AMPA receptors and regulate AMPA receptor trafficking in neurons. N-cadherin and β-catenin formed a protein complex with AMPA receptors in vivo, and this association was regulated by extracellular Ca²⁺. In addition, these proteins co-clustered at synapses in cultured neurons. In heterologous cells and in cultured neurons, overexpression of wild-type N-cadherin specifically increased the surface expression level of the AMPA receptor subunit glutamate receptor 1 (GluR1) and this effect was reversed by a dominant-negative form of N-cadherin. Finally, GluR1 increased the surface expression of N-cadherin in heterologous cells. Importantly, recent studies suggest that N-cadherin and β-catenin play key roles in structural plasticity in neurons. Therefore, our data suggest that the association of N-cadherin with AMPA receptors may serve as a biochemical link between structural and functional plasticity of synapses.
    Language English
    Size p. 652-661.
    Publishing place Blackwell Publishing Ltd
    Document type Article
    ZDB-ID 80158-6
    ISSN 1471-4159 ; 0022-3042 ; 1474-1644
    ISSN (online) 1471-4159
    ISSN 0022-3042 ; 1474-1644
    DOI 10.1111/j.1471-4159.2006.03740.x
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  6. Article ; Online: Identification of a new regulation pathway of EGFR and E-cadherin dynamics.

    Proux-Gillardeaux, Veronique / Advedissian, Tamara / Perin, Charlotte / Gelly, Jean-Christophe / Viguier, Mireille / Deshayes, Frederique

    Scientific reports

    2021  Volume 11, Issue 1, Page(s) 22705

    Abstract: ... therefore reveals that galectin-7 controls epidermal homeostasis through the regulation of E-cadherin/EGFR balance. ... trafficking allowing cell proliferation and migration control. In vivo observations further support ... E-cadherin and EGFR are known to be closely associated hence regulating differentiation and ...

    Abstract E-cadherin and EGFR are known to be closely associated hence regulating differentiation and proliferation notably in epithelia. We have previously shown that galectin-7 binds to E-cadherin and favors its retention at the plasma membrane. In this study, we shed in light that galectin-7 establishes a physical link between E-cadherin and EGFR. Indeed, our results demonstrate that galectin-7 also binds to EGFR, but unlike the binding to E-cadherin this binding is sugar dependent. The establishment of E-cadherin/EGFR complex and the binding of galectin-7 to EGFR thus lead to a regulation of its signaling and intracellular trafficking allowing cell proliferation and migration control. In vivo observations further support these results since an epidermal thickening is observed in galectin-7 deficient mice. This study therefore reveals that galectin-7 controls epidermal homeostasis through the regulation of E-cadherin/EGFR balance.
    MeSH term(s) Animals ; Antigens, CD/metabolism ; Cadherins/metabolism ; Cell Differentiation/genetics ; Cell Membrane/metabolism ; Cell Movement/genetics ; Cell Proliferation/genetics ; Epidermis/metabolism ; ErbB Receptors/metabolism ; Female ; Galectins/genetics ; Galectins/metabolism ; Gene Silencing ; HaCaT Cells ; Humans ; Mice ; Mice, Inbred C57BL ; Mice, Knockout ; Molecular Docking Simulation ; Signal Transduction/genetics
    Chemical Substances Antigens, CD ; CDH1 protein, human ; Cadherins ; Cdh1 protein, mouse ; Galectins ; LGALS7 protein, human ; Lgals7 protein, mouse ; EGFR protein, human (EC 2.7.10.1) ; EGFR protein, mouse (EC 2.7.10.1) ; ErbB Receptors (EC 2.7.10.1)
    Language English
    Publishing date 2021-11-22
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2615211-3
    ISSN 2045-2322 ; 2045-2322
    ISSN (online) 2045-2322
    ISSN 2045-2322
    DOI 10.1038/s41598-021-02042-3
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  7. Article ; Online: Regulation of ADAM10 by the TspanC8 Family of Tetraspanins and Their Therapeutic Potential.

    Harrison, Neale / Koo, Chek Ziu / Tomlinson, Michael G

    International journal of molecular sciences

    2021  Volume 22, Issue 13

    Abstract: ... of membrane proteins that interact with specific partner proteins to regulate their intracellular trafficking, lateral ... Notch, amyloid precursor protein, cadherins, and growth factors, and is important in health and ...

    Abstract The ubiquitously expressed transmembrane protein a disintegrin and metalloproteinase 10 (ADAM10) functions as a "molecular scissor", by cleaving the extracellular regions from its membrane protein substrates in a process termed ectodomain shedding. ADAM10 is known to have over 100 substrates including Notch, amyloid precursor protein, cadherins, and growth factors, and is important in health and implicated in diseases such as cancer and Alzheimer's. The tetraspanins are a superfamily of membrane proteins that interact with specific partner proteins to regulate their intracellular trafficking, lateral mobility, and clustering at the cell surface. We and others have shown that ADAM10 interacts with a subgroup of six tetraspanins, termed the TspanC8 subgroup, which are closely related by protein sequence and comprise Tspan5, Tspan10, Tspan14, Tspan15, Tspan17, and Tspan33. Recent evidence suggests that different TspanC8/ADAM10 complexes have distinct substrates and that ADAM10 should not be regarded as a single scissor, but as six different TspanC8/ADAM10 scissor complexes. This review discusses the published evidence for this "six scissor" hypothesis and the therapeutic potential this offers.
    MeSH term(s) ADAM10 Protein/physiology ; Amyloid Precursor Protein Secretases/physiology ; Animals ; Cadherins/metabolism ; Humans ; Membrane Proteins/metabolism ; Membrane Proteins/physiology ; Molecular Targeted Therapy/methods ; Tetraspanins/chemistry ; Tetraspanins/physiology
    Chemical Substances Cadherins ; Membrane Proteins ; Tetraspanins ; Amyloid Precursor Protein Secretases (EC 3.4.-) ; ADAM10 Protein (EC 3.4.24.81) ; ADAM10 protein, human (EC 3.4.24.81) ; Adam10 protein, mouse (EC 3.4.24.81)
    Language English
    Publishing date 2021-06-23
    Publishing country Switzerland
    Document type Journal Article ; Review
    ZDB-ID 2019364-6
    ISSN 1422-0067 ; 1422-0067 ; 1661-6596
    ISSN (online) 1422-0067
    ISSN 1422-0067 ; 1661-6596
    DOI 10.3390/ijms22136707
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  8. Article ; Online: Identification of a new regulation pathway of EGFR and E-cadherin dynamics

    Veronique Proux-Gillardeaux / Tamara Advedissian / Charlotte Perin / Jean-Christophe Gelly / Mireille Viguier / Frederique Deshayes

    Scientific Reports, Vol 11, Iss 1, Pp 1-

    2021  Volume 27

    Abstract: ... of E-cadherin/EGFR complex and the binding of galectin-7 to EGFR thus lead to a regulation ... through the regulation of E-cadherin/EGFR balance. ... of its signaling and intracellular trafficking allowing cell proliferation and migration control. In vivo ...

    Abstract Abstract E-cadherin and EGFR are known to be closely associated hence regulating differentiation and proliferation notably in epithelia. We have previously shown that galectin-7 binds to E-cadherin and favors its retention at the plasma membrane. In this study, we shed in light that galectin-7 establishes a physical link between E-cadherin and EGFR. Indeed, our results demonstrate that galectin-7 also binds to EGFR, but unlike the binding to E-cadherin this binding is sugar dependent. The establishment of E-cadherin/EGFR complex and the binding of galectin-7 to EGFR thus lead to a regulation of its signaling and intracellular trafficking allowing cell proliferation and migration control. In vivo observations further support these results since an epidermal thickening is observed in galectin-7 deficient mice. This study therefore reveals that galectin-7 controls epidermal homeostasis through the regulation of E-cadherin/EGFR balance.
    Keywords Medicine ; R ; Science ; Q
    Language English
    Publishing date 2021-11-01T00:00:00Z
    Publisher Nature Portfolio
    Document type Article ; Online
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  9. Article ; Online: Regulation of ADAM10 by the TspanC8 Family of Tetraspanins and Their Therapeutic Potential

    Neale Harrison / Chek Ziu Koo / Michael G. Tomlinson

    International Journal of Molecular Sciences, Vol 22, Iss 6707, p

    2021  Volume 6707

    Abstract: ... of membrane proteins that interact with specific partner proteins to regulate their intracellular trafficking, lateral ... Notch, amyloid precursor protein, cadherins, and growth factors, and is important in health and ...

    Abstract The ubiquitously expressed transmembrane protein a disintegrin and metalloproteinase 10 (ADAM10) functions as a “molecular scissor”, by cleaving the extracellular regions from its membrane protein substrates in a process termed ectodomain shedding. ADAM10 is known to have over 100 substrates including Notch, amyloid precursor protein, cadherins, and growth factors, and is important in health and implicated in diseases such as cancer and Alzheimer’s. The tetraspanins are a superfamily of membrane proteins that interact with specific partner proteins to regulate their intracellular trafficking, lateral mobility, and clustering at the cell surface. We and others have shown that ADAM10 interacts with a subgroup of six tetraspanins, termed the TspanC8 subgroup, which are closely related by protein sequence and comprise Tspan5, Tspan10, Tspan14, Tspan15, Tspan17, and Tspan33. Recent evidence suggests that different TspanC8/ADAM10 complexes have distinct substrates and that ADAM10 should not be regarded as a single scissor, but as six different TspanC8/ADAM10 scissor complexes. This review discusses the published evidence for this “six scissor” hypothesis and the therapeutic potential this offers.
    Keywords metalloproteinase ; ADAM10 ; tetraspanin ; TspanC8 ; membrane protein ; ectodomain shedding ; Biology (General) ; QH301-705.5 ; Chemistry ; QD1-999
    Subject code 612
    Language English
    Publishing date 2021-06-01T00:00:00Z
    Publisher MDPI AG
    Document type Article ; Online
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  10. Article ; Online: Novel Regulation of Integrin Trafficking by Rab11-FIP5 in Aggressive Prostate Cancer.

    Das, Lipsa / Gard, Jaime M C / Prekeris, Rytis / Nagle, Raymond B / Morrissey, Colm / Knudsen, Beatrice S / Miranti, Cindy K / Cress, Anne E

    Molecular cancer research : MCR

    2018  Volume 16, Issue 8, Page(s) 1319–1331

    Abstract: ... but the trafficking of α3β1 and α6β1 are distinct by an unknown mechanism. Using a mouse PDX tumor model containing ... as a lead candidate for α6β1 trafficking. Rab11-FIP5 and its membrane-binding domain were required for α6β1 ... like CD44, transferrin receptor, or E-cadherin. Depletion of Rab11-FIP5 resulted in the intracellular ...

    Abstract The laminin-binding integrins, α3β1 and α6β1, are needed for tumor metastasis and their surface expression is regulated by endocytic recycling. β1 integrins share the Rab11 recycling machinery, but the trafficking of α3β1 and α6β1 are distinct by an unknown mechanism. Using a mouse PDX tumor model containing human metastatic prostate cancer, Rab11 family interacting protein 5 (Rab11-FIP5) was identified as a lead candidate for α6β1 trafficking. Rab11-FIP5 and its membrane-binding domain were required for α6β1 recycling, without affecting the other laminin-binding integrin (i.e., α3β1) or unrelated membrane receptors like CD44, transferrin receptor, or E-cadherin. Depletion of Rab11-FIP5 resulted in the intracellular accumulation of α6β1 in the Rab11 recycling compartment, loss of cell migration on laminin, and an unexpected loss of α6β1 recycling in cell-cell locations. Taken together, these data demonstrate that α6β1 is distinct from α3β1 via Rab11-FIP5 recycling and recycles in an unexpected cell-cell location.
    MeSH term(s) Humans ; Integrin alpha5beta1/metabolism ; Male ; Prostatic Neoplasms/genetics ; Prostatic Neoplasms/metabolism ; rab GTP-Binding Proteins/metabolism
    Chemical Substances Integrin alpha5beta1 ; rab GTP-Binding Proteins (EC 3.6.5.2)
    Language English
    Publishing date 2018-05-14
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 2098788-2
    ISSN 1557-3125 ; 1541-7786
    ISSN (online) 1557-3125
    ISSN 1541-7786
    DOI 10.1158/1541-7786.MCR-17-0589
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