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Two Communication Bridges to One Versatile Molecule pp. 137-176 $100.00
Authors:  (Ricardo Mondragón, Doris Cerecedo, Departamento de Bioquímica, Unidad de Microscopía Electrónica, Centro de Investigación y de Estudios Avanzados (CINVESTAV) del IPN, México DF, México, and others)
Actin helical filaments are the key tools of the cytoskeleton for adapting cells to the
physical or chemical microenvironment signals organizing cell contents, coordinating
movement, or changing shape. Actin polymerization is controlled by regulatory proteins
including nucleation, depolymerizing and severing factors, capping proteins,
polymerases, crosslinkers, and stabilizing proteins. The cell’s exquisite sensitivity in
responding to a wide range of physical or chemical stimuli, is translated into cytoskeleton
reorganization and adhesion-site modulation.
Living cells survive, proliferate, or differentiate while they are anchored to their
extracellular matrix. It comprises a complex bulk of information integrated into a
coherent environmental signal. This is achieved through integrins that are the major
family of transmembrane adhesion receptors composed of α and β units. These
heterodimers not only play an anchorage mechanical role they also transmit chemical
signals into the cell concerning their microenvironment and adhesive state.
Integrin-based interaction networks follow an ordered series of events that range
from their activation to focal adhesion assembly involving the participation of actin and
actin binding proteins. Activated integrins link directly to the signalling and cytoskeletal
systems regulating multiple cellular features, such as cell anchoring, locomotion,
substrate deformation and matrix remodeling, in which actin possesses an essential role.
Integration of incoming signals and whether to respond to these depends not only on
integrin properties; an additional glycoprotein system named dystroglycan has
demonstrated specific binding patterns to certain extracellular matrix components,
supporting cell adhesion and translating signals. Dystroglycan was identified as
Dystrophin glycoprotein complex (DGC) component; it comprises α- and β subunits.
Alfa-dystroglycan is located at the extracellular peripheral membrane interacting with
extracellular matrix proteins, while β-dystroglycan binds to α-dystroglycan on the
extracellular face, and on its intracellular face to F-actin. Dystroglycan potential adhesion
is due to its privileged position between cytoskeleton and extracellular matrix combined
with their differential glycosylation patterns, tissue-specific expression, and multiple
potential interactions. In this regard, dystroglycan has been found as a component of
podosome adhesion structures, as well as in focal adhesions, interacting with vinexin, a
vinculin binding partner.
In this chapter, we focus on the relationship between the two specific transmembrane
proteins that link the extracellular matrix and connect with F-actin to develop
microenvironment-triggered responses, particularly regarding the focal adhesions, stress
fibers, podosomes, and filopodia in which integrins and dystroglycans are involved. 

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Two Communication Bridges to One Versatile Molecule pp. 137-176