期刊论文详细信息
Cell & Bioscience
Specific structure and unique function define the hemicentin
Williams B Isaacs7  Donald D Anthony1  Guifang Yan7  Yuexin Pan1  Edward Moharomd3  Odell B Jones5  Xin Zhou2  MengMeng Xu6  Xuehong Xu4 
[1] School of Medicine, Case Western Reserve University, Baltimore, MD, USA;School of Life Sciences, Shaanxi Normal University, Xi’an, Shaanxi 710062, China;School of Public Health, Johns Hopkins University, Baltimore, MD, USA;Previous affiliation: School of Medicine, University of Maryland, Baltimore, MD 21201, USA;School of Medicine, University of North Carolina, Chapel Hill, NC, USA;Duke University Medical Center, Durham, NC, USA;School of Medicine, Johns Hopkins University, Baltimore, MD, USA
关键词: Mitosis;    Cell division;    Tissue/Organ architecture;    Embryogenesis;    Hemicentin;    Fibulin;    Extracellular matrix (ECM);   
Others  :  791606
DOI  :  10.1186/2045-3701-3-27
 received in 2012-12-14, accepted in 2013-04-24,  发布年份 2013
PDF
【 摘 要 】

Hemicentin has come a long way from when it was first identified in C. elegans as him-4 (High incidence of males). The protein is now a recognized player in maintaining the architectural integrity of vertebrate tissues and organs. Highly conserved hemicentin sequences across species indicate this gene’s ancient evolutionary roots and functional importance. In mouse, hemicentin is liberally distributed on the cell surface of many cell types, including epithelial cells, endothelial cells of the eye, lung, and uterus, and trophectodermal cells of blastocyst. Recent discoveries have uncovered yet another vital purpose of hemicentin 1. The protein also serves a unique function in mitotic cytokinesis, during which this extracellular matrix protein plays a key role in cleavage furrow maturation. Though understanding of hemicentin function has improved through new discoveries, much about this protein remains mysterious.

【 授权许可】

   
2013 Xu et al.; licensee BioMed Central Ltd.

【 预 览 】
附件列表
Files Size Format View
20140705015438696.pdf 1271KB PDF download
Figure 3. 86KB Image download
Figure 2. 58KB Image download
Figure 1. 95KB Image download
【 图 表 】

Figure 1.

Figure 2.

Figure 3.

【 参考文献 】
  • [1]Colley MA, et al.: Fibulins. In The extracellular matrix an overview. Edited by Mecham RP. Berlin Heiderberg: Springer Verlag; 2011:337-367.
  • [2]de Vega S, et al.: TM14 is a new member of the fibulin family (fibulin-7) that interacts with extracellular matrix molecules and is active for cell binding. J Biol Chem 2007, 282(42):30878-30888.
  • [3]Argraves WS, et al.: Fibulins: physiological and disease perspectives. EMBO Rep 2003, 4(12):1127-1131.
  • [4]Hutter H, et al.: Conservation and novelty in the evolution of cell adhesion and extracellular matrix genes. Science 2000, 287(5455):989-994.
  • [5]C. elegans Sequencing Consortium: Genome sequence of the nematode C. elegans: a platform for investigating biology. Science 1998, 282(5396):2012-2018.
  • [6]Vogel BE, et al.: Hemicentin, a conserved extracellular member of the immune-globulin superfamily, organizes epithelial and other cell attachments into oriented line-shaped junctions. Development 2001, 128(6):883-894.
  • [7]Xu X, et al.: A secreted protein promotes cleavage furrow maturation during cytokinesis. Curr Biol 2011, 21(2):114-119.
  • [8]Jordan SN, et al.: Cytokinesis: thinking outside the cell. Curr Biol 2011, 21(3):R119-R121.
  • [9]Xu X, et al.: A new job for ancient extracellular matrix proteins: Hemicentins stabilize cleavage furrows. Commun Integr Biol 2011, 4(4):433-435.
  • [10]Vogel BE, et al.: Hemicentins: what have we learned from worms? Cell Res 2006, 16(11):872-878.
  • [11]Grabt RP: Control from without. The Scientist 2011. http://www.the-scientist.com/?articles.view/articleNo/30509/title/Control-from-Without/ webcite
  • [12]Argraves WS, et al.: Fibulin, a novel protein that interacts with the fibronectin receptor beta subunit cytoplasmic domain. Cell 1989, 58(4):623-629.
  • [13]Argraves WS, et al.: Fibulin is an extracellular matrix and plasma glycoprotein with repeated domain structure. J Cell Biol 1990, 111(6 Pt 2):3155-3164.
  • [14]Kluge M, et al.: Characterization of a novel calcium-binding 90-kDa glycoprotein (BM-90) shared by basement membranes and serum. Eur J Biochem 1990, 193(3):651-659.
  • [15]Pan TC, et al.: Sequence of extracellular mouse protein BM-90/fibulin and its calcium-dependent binding to other basement-membrane ligands. Eur J Biochem 1993, 215(3):733-740.
  • [16]Tran H, et al.: The self-association and fibronectin-binding sites of fibulin-1 map to calcium-binding epidermal growth factor-like domains. J Bio Chem 1997, 272(36):22600-22606.
  • [17]Gallagher WM, et al.: MBP1: a novel mutant p53-specific protein partner with oncogenic properties. Oncogene 1999, 18(24):3608-3616.
  • [18]Timpl R, et al.: Fibulins: a versatile family of extracellular matrix proteins. Nat Rev Mol Cell Biol 2003, 4(6):479-489.
  • [19]de Vega S, et al.: Fibulins: multiple roles in matrix structures and tissue functions. Cell Mol Life Sci 2009, 66(11–12):1890-1902.
  • [20]Segade F: Molecular evolution of the fibulins: implications on the functionality of the elastic fibulins. Gene 2010, 464(1–2):17-31.
  • [21]Carney TJ, et al.: Genetic analysis of fin development in zebrafish identifies furin and hemicentin1 as potential novel Fraser syndrome disease genes. PLoS Genet 2010, 6:e1000907.
  • [22]Muriel JM, et al.: Fibulin-1C and Fibulin-1D splice variants have distinct functions and assemble in a hemicentin-dependent manner. Development 2005, 132:4223-4234.
  • [23]Xu X, et al.: Hemicentins assemble on diverse epithelia in the mouse. J Histochem Cytochem 2007, 55(2):119-126.
  • [24]Feitosa NM, et al.: Hemicentin 2 and Fibulin 1 are required for epidermal-dermal junction formation and fin mesenchymal cell migration during zebrafish development. Dev Biol 2012, 369(2):235-248.
  文献评价指标  
  下载次数:26次 浏览次数:50次