The lamina-associated polypeptide 2 (LAP2) isoforms beta, gamma and omega of zebrafish: developmental expression and behavior during the cell cycle.
Zebrafish lamina-associated polypeptides 2 (ZLAP2) beta, gamma and omega have in common an N-terminal region with a LEM domain, and in the C-terminal half of the molecule a lamina binding domain and a membrane spanning sequence. The maternally synthesized omega is the largest isoform and the only LAP2 present in the rapidly dividing embryonic cells up to the gastrula stage. ZLAP2omega levels decrease during development, concomitant with the increase of the somatic isoforms ZLAP2beta and gamma. In somatic zebrafish cells ZLAP2gamma is the predominant isoform, whereas only small amounts of ZLAP2beta are present. During early embryonic development, ZLAP2omega becomes associated with mitotic chromosomes before anaphase. The surface of these chromosomes is decorated with vesicles, and each chromosome assembles its own nuclear envelope at the end of mitosis (karyomere formation). Ectopically expressed ZLAP2omega-green fluorescent protein (GFP) fusion protein targets vesicles to mitotic chromosomes in Xenopus A6 cells, suggesting that ZLAP2omega is involved in karyomere formation during early zebrafish development. When ZLAP2beta and gamma were expressed as GFP fusion proteins in Xenopus A6 cells, the beta- but not the gamma-isoform was found in association with mitotic chromosomes, and ZLAP2beta-containing chromosomes were decorated with vesicles. Further analysis of ZLAP2-GFP fusion proteins containing only distinct domains of the ZLAP2 isoforms revealed that the common N-terminal region in conjunction with beta- or omega-specific sequences mediate binding to mitotic chromosomes in vivo.
Division of Electron Microscopy, Biocenter of the University of Wü rzburg, Am Hubland, Germany.
Vera K
VK
Schoft
Ariane J
AJ
Beauvais
Carmen
C
Lang
Andreas
A
Gajewski
Kristina
K
Prüfert
Christoph
C
Winkler
Marie-Andrée
MA
Akimenko
Micheline
M
Paulin-Levasseur
Georg
G
Krohne
D000595:Amino Acid Sequence / Q000235:genetics; D000818:Animals; D001483:Base Sequence / Q000235:genetics; D001665:Binding Sites / Q000235:genetics; D002453:Cell Cycle / Q000235:genetics; D002460:Cell Line; D002875:Chromosomes / Q000235:genetics / Q000648:ultrastructure; D018076:DNA, Complementary / Q000032:analysis / Q000235:genetics; D004268:DNA-Binding Proteins / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism*; D004625:Embryo, Nonmammalian / Q000378:metabolism* / Q000648:ultrastructure; D018507:Gene Expression Regulation, Developmental / Q000235:genetics; D008565:Membrane Proteins / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism*; D008854:Microscopy, Electron; D008938:Mitosis / Q000235:genetics; D008969:Molecular Sequence Data; D009154:Mutation / Q000235:genetics; D009685:Nuclear Envelope / Q000235:genetics / Q000648:ultrastructure; D020033:Protein Isoforms / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism; D017434:Protein Structure, Tertiary / Q000235:genetics; D011993:Recombinant Fusion Proteins / Q000235:genetics / Q000378:metabolism; D013946:Thymopoietins / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism*; D014982:Xenopus laevis; D015027:Zebrafish / Q000196:embryology* / Q000378:metabolism*; D029961:Zebrafish Proteins / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism*
D018076:DNA, Complementary; D004268:DNA-Binding Proteins; D008565:Membrane Proteins; D020033:Protein Isoforms; D011993:Recombinant Fusion Proteins; D013946:Thymopoietins; D029961:Zebrafish Proteins; C093413:lamina-associated polypeptide 2; C483467:lamina-associated polypeptide 2, zebrafish