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XB-ART-49407
Mech Dev August 1, 2014; 133 203-17.

Diverse functions of kindlin/fermitin proteins during embryonic development in Xenopus laevis.

Rozario T , Mead PE , DeSimone DW .


Abstract
The kindlin/fermitin family includes three proteins involved in regulating integrin ligand-binding activity and adhesion. Loss-of-function mutations in kindlins1 and 3 have been implicated in Kindler Syndrome and Leukocyte Adhesion Deficiency III (LAD-III) respectively, whereas kindlin2 null mice are embryonic lethal. Post translational regulation of cell-cell and cell-ECM adhesion has long been presumed to be important for morphogenesis, however, few specific examples of activation-dependent changes in adhesion molecule function in normal development have been reported. In this study, antisense morpholinos were used to reduce expression of individual kindlins in Xenopus laevis embryos in order to investigate their roles in early development. Kindlin1 knockdown resulted in developmental delays, gross malformations of the gut and eventual lethality by tadpole stages. Kindlin2 morphant embryos displayed late stage defects in vascular maintenance and angiogenic branching consistent with kindlin2 loss of function in the mouse. Antisense morpholinos were also used to deplete maternal kindlin2 protein in oocytes and eggs. Embryos lacking maternal kindlin2 arrested at early cleavage stages due to failures in cytokinesis. Kindlin3 morphant phenotypes included defects in epidermal ciliary beating and partial paralysis at tailbud stages but these embryos recovered eventually as morpholino levels decayed. These results indicate a remarkably diverse range of kindlin functions in vertebrate development.

PubMed ID: 25173804
PMC ID: PMC4195491
Article link: Mech Dev
Grant support: [+]

Species referenced: Xenopus laevis
Genes referenced: aplnr cdh3 fermt1 fermt2 fermt3 grap2 hba1 hook3 kdr myc nkx2-5 prox1 tuba4b
Antibodies: Fermt2 Ab1 Fermt2 Ab2
Morpholinos: fermt1 MO1 fermt2 MO1 fermt3 MO1


Article Images: [+] show captions
References [+] :
Anthis, The tail of integrin activation. 2011, Pubmed