A. Schmidt et al., DESMOSOMES AND CYTOSKELETAL ARCHITECTURE IN EPITHELIAL DIFFERENTIATION - CELL-TYPE-SPECIFIC PLAQUE COMPONENTS AND INTERMEDIATE FILAMENT ANCHORAGE, European journal of cell biology, 65(2), 1994, pp. 229-245
Among the diverse kinds of intercellular, plaque bearing, cadherin con
taining junctions, desmosomes (maculae adhaerentes) represent a major
type characterized by the presence of specific transmembrane glycoprot
eins, i.e. desmosomal cadherins of the desmoglein and desmocollin cate
gories, and the cytoplasmic plaque proteins, desmoplakin I and plakogl
obin. Recent studies, however, have shown that the composition of desm
osomes is not identical in the various normal and tumorous desmosome-f
orming tissues and cell cultures, including diverse forms of epithelia
and carcinomas, meningothelia and meningiomas, myocardium and the lym
ph node follicle reticulum. Desmosomes can differ in their specific co
mplement of desmogleins, Dsg1-3, and desmocollins, Dsc1a-3b, as well a
s in the additional presence and in their relative amounts of certain
accessory plaque proteins such as desmoplakin II and plakophilin 1, a
basic member of the larger plakoglobin family of proteins (''band 6 pr
otein''). Assembly and function of desmosomes are effected by the inte
raction of the specific complement of desmosomal cadherins with certai
n cytoplasmic proteins. In particular, the cytoplasmic portions (''tai
ls'') of the desmosomal cadherins contain certain domains and amino ac
id sequence moths, identified by mutagenesis and transfection assays,
that are essential elements in desmosome formation, notably the assemb
ly of plaque proteins, and in the site-specific anchorage of intermedi
ate-sized filaments (IFs) of the cytoskeleton, thereby contributing to
the specific intracellular as well as supracellular, i.e. tissue, arc
hitecture.