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Cadherin Interactions
Published by Anonymous on 2007/9/27 (1466 reads)
1: Nat Rev Neurosci. 2007 Jan;8(1):11-20. Epub 2006 Nov 29.


The cadherin superfamily in neuronal connections and interactions.

Takeichi M.

RIKEN Center for Developmental Biology, 2-2-3 Minatojima-Minamimachi, Chuo-ku, Kobe 650-0047, Japan. takeichi@cdb.riken.jp

Neural development and the organization of complex neuronal circuits involve a number of processes that require cell-cell interaction. During these processes, axons choose specific partners for synapse formation and dendrites elaborate arborizations by interacting with other dendrites. The cadherin superfamily is a group of cell surface receptors that is comprised of more than 100 members. The molecular structures and diversity within this family suggest that these molecules regulate the contacts or signalling between neurons in a variety of ways. In this review I discuss the roles of three subfamilies - classic cadherins, Flamingo/CELSRs and protocadherins - in the regulation of neuronal recognition and connectivity.

Publication Types:
Research Support, Non-U.S. Gov't
Review

PMID: 17133224 [PubMed - indexed for MEDLINE]

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2: Methods Mol Biol. 2000;137:409-40.


Cadherin-mediated cell-cell interactions.

Knudsen KA, Soler AP.

Department of Biochemistry and Molecular Pharmacology, Lankenau Medical Research Center, Wynnewood, PA, USA.

Publication Types:
Review

PMID: 10948557 [PubMed - indexed for MEDLINE]

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3: J Pathol. 1997 Jun;182(2):128-37.


The interactions of APC, E-cadherin and beta-catenin in tumour development and progression.

Ilyas M, Tomlinson IP.

Cancer Genetics and Immunology Laboratory, Institute of Molecular Medicine, John Radcliffe Hospital, Oxford, Oxon, U.K.

Much progress has been made in identifying genes mutated during the development of colorectal carcinoma. Mutation of the APC gene in particular appears to be fundamental for colorectal tumour initiation. In contrast, loss of expression of E-cadherin appears to be a late event, which may be important in the development of invasion. Recent clarification of the function of APC, however, has shown that it exists in equilibrium with beta-catenin and E-cadherin. This review discusses the function of these molecules, their interactions, and how APC mutations may alter the equilibrium with beta-catenin and E-cadherin. It is argued that these changes cause aberrant architectural development of tissue, which results in loss of growth control. It is this escape from growth control, rather than acquisition of cell-autonomous growth, which results in the initial development of adenomas. The role of the E-cadherin-catenin unit in colorectal tumour invasion is discussed and the evidence is reviewed for the involvement of APC and E-cadherin in tumours arising from non-intestinal epithelia.

Publication Types:
Review

PMID: 9274521 [PubMed - indexed for MEDLINE]

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4: J Cell Biochem. 1996 Jun 15;61(4):514-23.


Cadherin-catenin complex: protein interactions and their implications for cadherin function.

Aberle H, Schwartz H, Kemler R.

Max-Planck-Institut für Immunbiologie, Freiburg, Germany.

Cadherins comprise a family of calcium-dependent glycoproteins that function in mediating cell-cell adhesion in virtually all solid tissues of multicellular organisms. In epithelial cells, E-cadherin represents a key molecule in the establishment and stabilization of cellular junctions. On the cellular level, E-cadherin is concentrated at the adherens junction and interacts homophilically with E-cadherin molecules of adjacent cells. Significant progress has been made in understanding the extra- and intracellular interactions of E-cadherin. Recent success in solving the three-dimensional structure of an extracellular cadherin domain provides a structural basis for understanding the homophilic interaction mechanism and the calcium requirement of cadherins. According to the crystal structure, individual cadherin molecules cooperate to form a linear cell adhesion zipper. The intracellular anchorage of cadherins is regulated by the dynamic association with cytoplasmic proteins, termed catenins. The cytoplasmic domain of E-cadherin is complexed with either beta-catenin or plakoglobin (gamma-catenin). Beta-catenin and plakoglobin bind directly to alpha-catenin, giving rise to two distinct cadherin-catenin complexes (CCC). Alpha-catenin is thought to link both CCC's to actin filaments. The anchorage of cadherins to the cytoskeleton appears to be regulated by tyrosine phosphorylation. Phosphorylation-induced junctional disassembly targets the catenins, indicating that catenins are components of signal transduction pathways. The unexpected association of catenins with the product of the tumor suppressor gene APC has led to the discovery of a second, cadherin-independent catenin complex. Two separate catenin complexes are therefore involved in the cross-talk between cell adhesion and signal transduction. In this review we focus on protein interactions regulating the molecular architecture and function of the CCC. In the light of a fundamental role of the CCC during mammalian development and tissue morphogenesis, we also discuss the phenotypes of embryos lacking E-cadherin or beta-catenin.

Publication Types:
Review

PMID: 8806074 [PubMed - indexed for MEDLINE]

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5: Proc Natl Acad Sci U S A. 1994 Nov 8;91(23):10759-61.


Comment in:
Proc Natl Acad Sci U S A. 1994 Nov 8;91(23):10790-4.

Unraveling the cytoplasmic interactions of the cadherin superfamily.

Cowin P.

Department of Cell Biology, New York University Medical Center, NY 10016.

Publication Types:
Review

PMID: 7971957 [PubMed - indexed for MEDLINE]
 

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