title: Apical accumulation of MARCKS in neural plate cells during neurulation in the chick embryo.
abstract: BACKGROUND
  The neural tube is formed by morphogenetic movements largely dependent on cytoskeletal dynamics. Actin and many of its associated proteins have been proposed as important mediators of neurulation. For instance, mice deficient in MARCKS, an actin cross-linking membrane-associated protein that is regulated by PKC and other kinases, present severe developmental defects, including failure of cranial neural tube closure.
  
  
  RESULTS
  To determine the distribution of MARCKS, and its possible relationships with actin during neurulation, chick embryos were transversely sectioned and double labeled with an anti-MARCKS polyclonal antibody and phalloidin. In the neural plate, MARCKS was found ubiquitously distributed at the periphery of the cells, being conspicuously accumulated in the apical cell region, in close proximity to the apical actin meshwork. This asymmetric distribution was particularly noticeable during the bending process. After the closure of the neural tube, the apically accumulated MARCKS disappeared, and this cell region became analogous to the other peripheral cell zones in its MARCKS content. Actin did not display analogous variations, remaining highly concentrated at the cell subapical territory. The transient apical accumulation of MARCKS was found throughout the neural tube axis. The analysis of another epithelial bending movement, during the formation of the lens vesicle, revealed an identical phenomenon.
  
  
  CONCLUSIONS
  MARCKS is transiently accumulated at the apical region of neural plate and lens placode cells during processes of bending. This asymmetric subcellular distribution of MARCKS starts before the onset of neural plate bending. These results suggest possible upstream regulatory actions of MARCKS on some functions of the actin subapical meshwork.
authors.affiliation: Laboratorio de Cultivo de Tejidos, Sección Biología Celular, Facultad de Ciencias, Universidad de la República, Montevideo, Uruguay. fzolessi@fcien.edu.uy
authors.forename: F R
authors.initials: FR
authors.lastname: Zolessi
authors.forename: C
authors.initials: C
authors.lastname: Arruti
mesh_terms: D000199:Actins / Q000378:metabolism; D000818:Animals; D030161:Avian Proteins / Q000378:metabolism; D002490:Central Nervous System / Q000196:embryology*; D002642:Chick Embryo / Q000294:innervation* / Q000378:metabolism*; D016616:Cryoultramicrotomy; D004847:Epithelial Cells / Q000378:metabolism; D005260:Female; D047908:Intracellular Signaling Peptides and Proteins; D007908:Lens, Crystalline / Q000196:embryology / Q000378:metabolism; D008565:Membrane Proteins; D000076250:Myristoylated Alanine-Rich C Kinase Substrate; D009419:Nerve Tissue Proteins / Q000378:metabolism; D010750:Phosphoproteins / Q000378:metabolism*; D016548:Prosencephalon / Q000196:embryology / Q000378:metabolism / Q000502:physiology; D012249:Rhombencephalon / Q000196:embryology / Q000378:metabolism / Q000502:physiology; D013131:Spine / Q000196:embryology / Q000378:metabolism / Q000502:physiology; D013194:Staining and Labeling; D015053:Zygote
chemical_list: D000199:Actins; D030161:Avian Proteins; D047908:Intracellular Signaling Peptides and Proteins; C000619711:Marcks protein, mouse; D008565:Membrane Proteins; D009419:Nerve Tissue Proteins; D010750:Phosphoproteins; D000076250:Myristoylated Alanine-Rich C Kinase Substrate