Collagen XXII binds to collagen-binding integrins via the novel motifs GLQGER and GFKGER

2014 ◽  
Vol 459 (1) ◽  
pp. 217-227 ◽  
Author(s):  
Daniela Zwolanek ◽  
Guido Veit ◽  
Johannes A. Eble ◽  
Donald Gullberg ◽  
Florence Ruggiero ◽  
...  
Keyword(s):  
Cell Attachment ◽  
Hacat Cells ◽  
The Novel ◽  
Collagen Binding ◽  
Binding Motifs ◽  
Helical Domain ◽  
Triple Helical Domain

Cell attachment to collagens is mediated by integrins. In the present study, we define two new integrin-binding motifs, GLQGER and GFKGER, within the collagen XXII triple helical domain. Mutation of the two motifs in collagen XXII abolishes the binding to HaCaT cells completely.

The fibril structure of type V collagen triple-helical domain

Micron ◽  
2001 ◽  
Vol 32 (3) ◽  
pp. 317-323 ◽  
Author(s):  
K Mizuno ◽  
E Adachi ◽  
Y Imamura ◽  
O Katsumata ◽  
T Hayashi
Keyword(s):  
Type V Collagen ◽  
Helical Domain ◽  
Fibril Structure ◽  
Triple Helical Domain ◽  
Type V

The novel murine calmodulin-binding protein Sha1 disrupts mitotic spindle and replication checkpoint functions in fission yeast

1998 ◽  
Vol 111 (24) ◽  
pp. 3609-3619
Author(s):  
R. Craig ◽  
C. Norbury
Keyword(s):  
Fission Yeast ◽  
Mitotic Spindle ◽  
Binding Protein ◽  
Protein S ◽  
Spindle Pole ◽  
The Novel ◽  
Checkpoint Control ◽  
Binding Motifs ◽  
Replication Checkpoint ◽  
Calmodulin Binding

Entry into mitosis is normally blocked in eukaryotic cells that have not completed replicative DNA synthesis; this ‘S-M’ checkpoint control is fundamental to the maintenance of genomic integrity. Mutants of the fission yeast Schizosaccharomyces pombe defective in the S-M checkpoint fail to arrest the cell cycle when DNA replication is inhibited and hence attempt mitosis and cell division with unreplicated chromosomes, resulting in the ‘cut’ phenotype. In an attempt to identify conserved molecules involved in the S-M checkpoint we have screened a regulatable murine cDNA library in S. pombe and have identified cDNAs that induce the cut phenotype in cells arrested in S phase by hydroxyurea. One such cDNA encodes a novel protein with multiple calmodulin-binding motifs that, in addition to its effects on the S-M checkpoint, perturbed mitotic spindle functions, although spindle pole duplication was apparently normal. Both aspects of the phenotype induced by this cDNA product, which we term Sha1 (for spindle and hydroxyurea checkpoint abnormal), were suppressed by simultaneous overexpression of calmodulin. Sha1 is structurally related to the product of the Drosophila gene abnormal spindle (asp). These data suggest that calmodulin-binding protein(s) are important in the co-ordination of mitotic spindle functions with mitotic entry in fission yeast, and probably also in multicellular eukaryotes.

scholarly journals Large Deletions Targeting the Triple-Helical Domain of Collagen VII Lead to Mild Acral Dominant Dystrophic Epidermolysis Bullosa

2018 ◽  
Vol 138 (4) ◽  
pp. 987-991 ◽  
Author(s):  
Nadja Chmel ◽  
Olivier Bornert ◽  
Ingrid Hausser ◽  
Gabriele Grüninger ◽  
Wiktor Borozkin ◽  
...  
Keyword(s):  
Epidermolysis Bullosa ◽  
Dystrophic Epidermolysis Bullosa ◽  
Helical Domain ◽  
Large Deletions ◽  
Triple Helical Domain ◽  
Collagen Vii
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