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MACF1
Microtubule-actin cross-linking factor 1, isoforms 1/2/3/5 is a protein that in humans is encoded by the ''MACF1'' gene.
MACF1 encodes a large protein containing numerous spectrin and leucine-rich repeat (LRR) domains. MACF1 is a member of a family of proteins that form bridges between different cytoskeletal elements. This protein facilitates actin-microtubule interactions at the cell periphery and couples the microtubule network to cellular junctions.〔(【引用サイトリンク】 url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=23499 )〕
MACF1 belongs to a subset of +TIPs or proteins which bind to growing microtubule ends called spectraplakins. Spectraplakins characteristically have distinctive microtubule and actin binding domains, which allow MACF1 to bind to both cytoskeletal elements.〔 MACF1 goes by many names and is also called ACF7 or actin cross-linking factor 7, MACF, macrophin, trabeculin α, and ABP620. Alternatively spliced transcript variants encoding distinct isoforms of MACF1 have been described.〔 MACF1 is also an important protein for cell migration in processes such as wound healing.
==Structure==
MACF1 is an enormous protein of 5380 amino acid residues. The N-terminal segment has an actin binding domain and the C-terminal segment has a +TIP binding site as well as microtubule interacting domains. This allows MACF1 to crosslink both actin and microtubules. The C-terminal region contains both a Gas2-related domain and a GSR-repeat domain, which both are involved with interacting with microtubules. The C-terminus of MACF1 is thought to associate to the microtubule lattice through the acidic C-terminal tails of tubulin subunits.〔 However, MACF1 does not always associate with the microtubule directly, and also binds through many proteins which localize at the microtubule plus end. Such proteins include EB1, CLASP1, and CLASP2, whose interactions with MACF1 were determined through coimmunoprecipitation assay.〔 Not only does MACF1's C-terminal tail bind to microtubules, but it also has key phosphorylation sites. When these sites are phosphorylated by its regulator GSK3β, the ability of MACF1 to bind to microtubules is disrupted.〔 MACF1 also has an actin-regulated ATPase domain, which is approximately 3000 amino acid residues long in the C-terminal region, and is responsible for cytoskeletal dynamics.〔
抄文引用元・出典: フリー百科事典『 ウィキペディア（Wikipedia）』
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