Bullous pemphigoid antigen 1, encoded by the dystonin gene, is a member of the plakin family of cytolinkers. This protein family connects the intermediate filament, microtubule and microfilament cytoskeletal networks with each other and to distinct cell membrane sites and act as scaffolds and adaptors for signaling proteins that modulate cytoskeletal dynamics, cell migration, differentiation, and stress responses. Multiple transcription initiation sites and alternative splicing of Dst results in three major BPAG1 isoforms, BPAG1a, BPAG1b, and BPAG1e, which exhibit different tissue-specific expression profiles and functions. Furthermore, at least three alternative transcription start sites give rise to several Dst mRNA variants encoding different N-terminal BPAG1a/b isoforms. While BPAG1e is found in stratified epithelia, BPAG1a and b are predominantly expressed in neurons and in striated muscles, respectively. BPAG1a/b are homologous to the mammalian microtubule actin cross-linking factor 1 isoforms a and b, and to Drosophila Short stop. MACF1a and Shot are important for MT network structure maintenance. Shot, BPAG1a/b and MACF1a/b differ from the other plakins by having a unique rod Cefprozil hydrate domain that consists of spectrin repeats, in addition to the SRs that make up the common plakin domain. These proteins are therefore also called spectraplakins. The BPAG1a/b isoforms are made up of multiple modular domains. They possess an actin-5-Aminolevulinic acid hydrochloride binding domain and a plakin domain in their N-terminus, and an MT-binding domain in their C-terminus. The latter is composed of a growth arrest-specific protein 2 related domain, which binds to and stabilizes MTs and a glycine-serine-arginine repeat-containing region, which bundles MTs. In addition, the C-terminal extremity of BPAG1a/b is able to form a complex with end-binding protein 1. EB1 is a core component of the MT plus end complexes, which autonomously tracks MT plus ends and recruits other proteins. Furthermore, BPAG1a is a binding partner of p150Glued subunit of dynactin, which also interacts with MT plus end proteins. Dynactin is thought to mediate the binding of dynein to cargos such as membranous organelles.