Advanced SearchSearch Tips
Isoforms, structures, and functions of versatile spectraplakin MACF1
facebook(new window)  Pirnt(new window) E-mail(new window) Excel Download
  • Journal title : BMB Reports
  • Volume 49, Issue 1,  2016, pp.37-44
  • Publisher : Korean Society for Biochemistry and Molecular Biology
  • DOI : 10.5483/BMBRep.2016.49.1.185
 Title & Authors
Isoforms, structures, and functions of versatile spectraplakin MACF1
Hu, Lifang; Su, Peihong; Li, Runzhi; Yin, Chong; Zhang, Yan; Shang, Peng; Yang, Tuanmin; Qian, Airong;
  PDF(new window)
Spectraplakins are crucially important communicators, linking cytoskeletal components to each other and cellular junctions. Microtubule actin crosslinking factor 1 (MACF1), also known as actin crosslinking family 7 (ACF7), is a member of the spectraplakin family. It is expressed in numerous tissues and cells as one extensively studied spectraplakin. MACF1 has several isoforms with unique structures and well-known function to be able to crosslink F-actin and microtubules. MACF1 is one versatile spectraplakin with various functions in cell processes, embryo development, tissue-specific functions, and human diseases. The importance of MACF1 has become more apparent in recent years. Here, we summarize the current knowledge on the presence and function of MACF1 and provide perspectives on future research of MACF1 based on our studies and others. [BMB Reports 2016; 49(1): 37-44]
 Cited by
BPAG1 in muscles: Structure and function in skeletal, cardiac and smooth muscle, Seminars in Cell & Developmental Biology, 2017, 69, 26  crossref(new windwow)
Microtubule actin cross-linking factor 1, a novel target in glioblastoma, International Journal of Oncology, 2017, 50, 1, 310  crossref(new windwow)
Microtubule actin crosslinking factor 1 promotes osteoblast differentiation by promoting β-catenin/TCF1/Runx2 signaling axis, Journal of Cellular Physiology, 2017  crossref(new windwow)
The role of MACF1 in nervous system development and maintenance, Seminars in Cell & Developmental Biology, 2017, 69, 9  crossref(new windwow)
Microtubule actin cross-linking factor 1, a novel potential target in cancer, Cancer Science, 2017  crossref(new windwow)
MACF1, versatility in tissue-specific function and in human disease, Seminars in Cell & Developmental Biology, 2017, 69, 3  crossref(new windwow)
MicroRNA targeting microtubule cross-linked protein (MACF1) would suppress the invasion and metastasis of malignant tumor, Medical Hypotheses, 2017, 104, 25  crossref(new windwow)
Suozzi KC, Wu X and Fuchs E (2012) Spectraplakins: master orchestrators of cytoskeletal dynamics. J Cell Biol 197, 465-475 crossref(new window)

Huelsmann S and Brown NH (2014) Spectraplakins. Curr Biol 24, R307-308 crossref(new window)

Roper K, Gregory SL and Brown NH (2002) The 'spectraplakins': cytoskeletal giants with characteristics of both spectrin and plakin families. J Cell Sci 115, 4215-4225 crossref(new window)

Sonnenberg A and Liem RK (2007) Plakins in development and disease. Exp Cell Res 313, 2189-2203 crossref(new window)

Kodama A, Karakesisoglou I, Wong E, Vaezi A and Fuchs E (2003) ACF7: an essential integrator of microtubule dynamics. Cell 115, 343-354 crossref(new window)

Wu X, Kodama A and Fuchs E (2008) ACF7 regulates cytoskeletal-focal adhesion dynamics and migration and has ATPase activity. Cell 135, 137-148 crossref(new window)

Wu X, Shen QT, Oristian DS et al (2011) Skin stem cells orchestrate directional migration by regulating microtubule-ACF7 connections through GSK3β. Cell 144, 341-352 crossref(new window)

Ka M, Jung EM, Mueller U and Kim WY (2014) MACF1 regulates the migration of pyramidal neurons via microtubule dynamics and GSK-3 signaling. Dev Biol 395, 4-18 crossref(new window)

Roper K and Brown NH (2003) Maintaining epithelial integrity: a function for gigantic spectraplakin isoforms in adherens junctions. J Cell Biol 162, 1305-1315 crossref(new window)

Bouameur JE, Favre B and Borradori L (2014) Plakins, a versatile family of cytolinkers: roles in skin integrity and in human diseases. J Invest Dermatol 134, 885-894 crossref(new window)

Chen HJ, Lin CM, Lin CS, Perez-Olle R, Leung CL and Liem RK (2006) The role of microtubule actin cross-linking factor 1 (MACF1) in the Wnt signaling pathway. Genes Dev 20, 1933-1945 crossref(new window)

Jorgensen LH, Mosbech MB, Faergeman NJ, Graakjaer J, Jacobsen SV and Schroder HD (2014) Duplication in the microtubule-actin cross-linking factor 1 gene causes a novel neuromuscular condition. Sci Rep 4, 5180 crossref(new window)

Byers TJ, Beggs AH, McNally EM and Kunkel LM (1995) Novel actin crosslinker superfamily member identified by a two step degenerate PCR procedure. FEBS Lett 368, 500-504 crossref(new window)

Bernier G, Mathieu M, De Repentigny Y, Vidal SM and Kothary R (1996) Cloning and characterization of mouse ACF7, a novel member of the dystonin subfamily of actin binding proteins. Genomics 38, 19-29 crossref(new window)

Leung CL, Sun D, Zheng M, Knowles DR and Liem RK (1999) Microtubule actin cross-linking factor (MACF): a hybrid of dystonin and dystrophin that can interact with the actin and microtubule cytoskeletons. J Cell Biol 147, 1275-1286 crossref(new window)

Okuda T, Matsuda S, Nakatsugawa S et al (1999) Molecular cloning of macrophin, a human homologue of Drosophila kakapo with a close structural similarity to plectin and dystrophin. Biochem Biophys Res Commun 264, 568-574 crossref(new window)

Sun Y, Zhang J, Kraeft SK et al (1999) Molecular cloning and characterization of human trabeculin-alpha, a giant protein defining a new family of actin-binding proteins. J Biol Chem 274, 33522-33530 crossref(new window)

Gong TW, Besirli CG and Lomax MI (2001) MACF1 gene structure: a hybrid of plectin and dystrophin. Mamm Genome 12, 852-861 crossref(new window)

Brown A, Bernier G, Mathieu M, Rossant J and Kothary R (1995) The mouse dystonia musculorum gene is a neural isoform of bullous pemphigoid antigen 1. Nat Genet 10, 301-306 crossref(new window)

Leung CL, Zheng M, Prater SM and Liem RK (2001) The BPAG1 locus: Alternative splicing produces multiple isoforms with distinct cytoskeletal linker domains, including predominant isoforms in neurons and muscles. J Cell Biol 154, 691-697 crossref(new window)

Lin CM, Chen HJ, Leung CL, Parry DA and Liem RK (2005) Microtubule actin crosslinking factor 1b: a novel plakin that localizes to the Golgi complex. J Cell Sci 118, 3727-3738 crossref(new window)

Goryunov D, He CZ, Lin CS, Leung CL and Liem RK (2010) Nervous-tissue-specific elimination of microtubule-actin crosslinking factor 1a results in multiple developmental defects in the mouse brain. Mol Cell Neurosci 44, 1-14 crossref(new window)

Sun D, Leung CL and Liem RK (2001) Characterization of the microtubule binding domain of microtubule actin crosslinking factor (MACF): identification of a novel group of microtubule associated proteins. J Cell Sci 114, 161-172

Bernier G, Pool M, Kilcup M, Alfoldi J, De Repentigny Y and Kothary R (2000) Acf7 (MACF) is an actin and microtubule linker protein whose expression predominates in neural, muscle, and lung development. Dev Dyn 219, 216-225 crossref(new window)

Karakesisoglou I, Yang Y and Fuchs E (2000) An epidermal plakin that integrates actin and microtubule networks at cellular junctions. J Cell Biol 149, 195-208 crossref(new window)

Way M, Pope B and Weeds AG (1992) Evidence for functional homology in the F-actin binding domains of gelsolin and alpha-actinin: implications for the requirements of severing and capping. J Cell Biol 119, 835-842 crossref(new window)

Winder SJ, Hemmings L, Maciver SK et al (1995) Utrophin actin binding domain: analysis of actin binding and cellular targeting. J Cell Sci 108 (Pt 1), 63-71

Bandi S, Singh SM and Mallela KM (2015) Interdomain linker determines primarily the structural stability of dystrophin and utrophin tandem calponin-homology domains rather than their actin-binding affinity. Biochemistry 54, 5480-5488 crossref(new window)

Jefferson JJ, Leung CL and Liem RK (2004) Plakins: goliaths that link cell junctions and the cytoskeleton. Nat Rev Mol Cell Biol 5, 542-553 crossref(new window)

Jefferson JJ, Ciatto C, Shapiro L and Liem RK (2007) Structural analysis of the plakin domain of bullous pemphigoid antigen1 (BPAG1) suggests that plakins are members of the spectrin superfamily. J Mol Biol 366, 244-257 crossref(new window)

Sonnenberg A, Rojas AM and de Pereda JM (2007) The structure of a tandem pair of spectrin repeats of plectin reveals a modular organization of the plakin domain. J Mol Biol 368, 1379-1391 crossref(new window)

Rezniczek GA, de Pereda JM, Reipert S and Wiche G (1998) Linking integrin α6β4-based cell adhesion to the intermediate filament cytoskeleton: direct interaction between the β4 subunit and plectin at multiple molecular sites. J Cell Biol 141, 209-225 crossref(new window)

Koster J, Geerts D, Favre B, Borradori L and Sonnenberg A (2003) Analysis of the interactions between BP180, BP230, plectin and the integrin α6β4 important for hemidesmosome assembly. J Cell Sci 116, 387-399 crossref(new window)

Hopkinson SB and Jones JC (2000) The N terminus of the transmembrane protein BP180 interacts with the N-terminal domain of BP230, thereby mediating keratin cytoskeleton anchorage to the cell surface at the site of the hemidesmosome. Mol Biol Cell 11, 277-286 crossref(new window)

Favre B, Fontao L, Koster J et al (2001) The hemidesmosomal protein bullous pemphigoid antigen 1 and the integrin β4 subunit bind to ERBIN. Molecular cloning of multiple alternative splice variants of ERBIN and analysis of their tissue expression. J Biol Chem 276, 32427-32436 crossref(new window)

Yan Y, Winograd E, Viel A, Cronin T, Harrison SC and Branton D (1993) Crystal structure of the repetitive segments of spectrin. Science 262, 2027-2030 crossref(new window)

Pascual J, Pfuhl M, Walther D, Saraste M and Nilges M (1997) Solution structure of the spectrin repeat: a left-handed antiparallel triple-helical coiled-coil. J Mol Biol 273, 740-751 crossref(new window)

Choi HJ, Park-Snyder S, Pascoe LT, Green KJ and Weis WI (2002) Structures of two intermediate filament-binding fragments of desmoplakin reveal a unique repeat motif structure. Nat Struct Biol 9, 612-620

Green KJ, Parry DA, Steinert PM et al (1990) Structure of the human desmoplakins. Implications for function in the desmosomal plaque. J Biol Chem 265, 2603-2612

Zaoui K, Benseddik K, Daou P, Salaun D and Badache A (2010) ErbB2 receptor controls microtubule capture by recruiting ACF7 to the plasma membrane of migrating cells. Proc Natl Acad Sci U S A 107, 18517-18522 crossref(new window)

Margaron Y, Fradet N and Cote JF (2013) ELMO recruits actin cross-linking family 7 (ACF7) at the cell membrane for microtubule capture and stabilization of cellular protrusions. J Biol Chem 288, 1184-1199 crossref(new window)

Burgo A, Proux-Gillardeaux V, Sotirakis E et al (2012) A molecular network for the transport of the TI-VAMP/VAMP7 vesicles from cell center to periphery. Dev Cell 23, 166-180 crossref(new window)

Sohda M, Misumi Y, Ogata S et al (2015) Trans-Golgi protein p230/golgin-245 is involved in phagophore formation. Biochem Biophys Res Commun 456, 275-281 crossref(new window)

Liu P, Wakamiya M, Shea MJ, Albrecht U, Behringer RR and Bradley A (1999) Requirement for Wnt3 in vertebrate axis formation. Nat Genet 22, 361-365 crossref(new window)

Kelly OG, Pinson KI and Skarnes WC (2004) The Wnt co-receptors Lrp5 and Lrp6 are essential for gastrulation in mice. Development 131, 2803-2815 crossref(new window)

Gupta T, Marlow FL, Ferriola D et al (2010) Microtubule actin crosslinking factor 1 regulates the Balbiani body and animal-vegetal polarity of the zebrafish oocyte. PLoS Genet 6, e1001073 crossref(new window)

Prokop A, Uhler J, Roote J and Bate M (1998) The kakapo mutation affects terminal arborization and central dendritic sprouting of Drosophila motorneurons. J Cell Biol 143, 1283-1294 crossref(new window)

Sanchez-Soriano N, Travis M, Dajas-Bailador F, Goncalves-Pimentel C, Whitmarsh AJ and Prokop A (2009) Mouse ACF7 and drosophila short stop modulate filopodia formation and microtubule organisation during neuronal growth. J Cell Sci 122, 2534-2542 crossref(new window)

Munemasa Y, Chang CS, Kwong JM et al (2012) The neuronal EGF-related gene Nell2 interacts with Macf1 and supports survival of retinal ganglion cells after optic nerve injury. PLoS One 7, e34810 crossref(new window)

Collard JF and Hinsenkamp M (2015) Cellular processes involved in human epidermal cells exposed to extremely low frequency electric fields. Cell Signal 27, 889-898 crossref(new window)

Qian AR, Hu LF, Gao X et al (2009) Large gradient high magnetic field affects the association of MACF1 with actin and microtubule cytoskeleton. Bioelectromagnetics 30, 545-555 crossref(new window)

Hu LF, Su PH, Li RZ et al (2015) Knockdown of microtubule actin crosslinking factor 1 inhibits cell proliferation in MC3T3-E1 osteoblastic cells. BMB Rep 48, 583-588 crossref(new window)

Fassett JT, Xu X, Kwak D et al (2013) Microtubule Actin Cross-linking Factor 1 regulates cardiomyocyte microtubule distribution and adaptation to hemodynamic overload. PLoS One 8, e73887 crossref(new window)

Liang Y, Shi C, Yang J et al (2013) ACF7 regulates colonic permeability. Int J Mol Med 31, 861-866 crossref(new window)

Sjoblom T, Jones S, Wood LD et al (2006) The consensus coding sequences of human breast and colorectal cancers. Science 314, 268-274 crossref(new window)

Zhang J, Wu G, Miller CP et al (2013) Whole-genome sequencing identifies genetic alterations in pediatric lowgrade gliomas. Nat Genet 45, 602-612 crossref(new window)

Fleischer T, Frigessi A, Johnson KC et al (2014) Genomewide DNA methylation profiles in progression to in situ and invasive carcinoma of the breast with impact on gene transcription and prognosis. Genome Biol 15, 435

Del Valle PR, Milani C, Brentani MM et al (2014) Transcriptional profile of fibroblasts obtained from the primary site, lymph node and bone marrow of breast cancer patients. Genet Mol Biol 37, 480-489 crossref(new window)

Stransky N, Cerami E, Schalm S, Kim JL and Lengauer C (2014) The landscape of kinase fusions in cancer. Nat Commun 5, 4846 crossref(new window)