Crystal structure of a calponin homology domain

1997 ◽  
Vol 4 (3) ◽  
pp. 175-179 ◽  
Author(s):  
Kristina Djinovic Carugo ◽  
Sonia Bañuelos ◽  
Matti Saraste
Keyword(s):  
Crystal Structure ◽  
Calponin Homology Domain ◽  
Calponin Homology

scholarly journals Endothelial IQGAP1 regulates leukocyte transmigration by directing the LBRC to the site of diapedesis

2019 ◽  
Vol 216 (11) ◽  
pp. 2582-2601 ◽  
Author(s):  
David P. Sullivan ◽  
Prarthana J. Dalal ◽  
Fanny Jaulin ◽  
David B. Sacks ◽  
Geri Kreitzer ◽  
...  
Keyword(s):  
Endothelial Cells ◽  
Scaffold Protein ◽  
Interacting Proteins ◽  
Calponin Homology Domain ◽  
Directed Movement ◽  
Lateral Border ◽  
Leukocyte Transmigration ◽  
Calponin Homology ◽  
First Time

Transendothelial migration (TEM) of leukocytes across the endothelium is critical for inflammation. In the endothelium, TEM requires the coordination of membrane movements and cytoskeletal interactions, including, prominently, recruitment of the lateral border recycling compartment (LBRC). The scaffold protein IQGAP1 was recently identified in a screen for LBRC-interacting proteins. Knockdown of endothelial IQGAP1 disrupted the directed movement of the LBRC and substantially reduced leukocyte TEM. Expression of truncated IQGAP1 constructs demonstrated that the calponin homology domain is required for IQGAP1 localization to endothelial borders and that the IQ domain, on the same IQGAP1 polypeptide, is required for its function in TEM. This is the first reported function of IQGAP1 requiring two domains to be present on the same polypeptide. Additionally, we show for the first time that IQGAP1 in the endothelium is required for efficient TEM in vivo. These findings reveal a novel function for IQGAP1 and demonstrate that IQGAP1 in endothelial cells facilitates TEM by directing the LBRC to the site of TEM.

scholarly journals Tropomyosin-binding properties of the CHASM protein are dependent upon its calponin homology domain

FEBS Letters ◽  
2010 ◽  
Vol 584 (15) ◽  
pp. 3311-3316 ◽  
Author(s):  
Annegret Ulke-Lemée ◽  
Hiroaki Ishida ◽  
Meredith A. Borman ◽  
Alexandra Valderrama ◽  
Hans J. Vogel ◽  
...  
Keyword(s):  
Calponin Homology Domain ◽  
Binding Properties ◽  
Calponin Homology

scholarly journals Molecular Basis of Tubulin Transport Within the Cilium by IFT74 and IFT81

Science ◽  
2013 ◽  
Vol 341 (6149) ◽  
pp. 1009-1012 ◽  
Author(s):  
Sagar Bhogaraju ◽  
Lukas Cajanek ◽  
Cécile Fort ◽  
Thierry Blisnick ◽  
Kristina Weber ◽  
...  
Keyword(s):  
Molecular Basis ◽  
Molecular Mechanisms ◽  
Intraflagellar Transport ◽  
Human Cells ◽  
Eukaryotic Cells ◽  
Calponin Homology Domain ◽  
Basic Domain ◽  
Calponin Homology ◽  
Tubulin Binding

Intraflagellar transport (IFT) of ciliary precursors such as tubulin from the cytoplasm to the ciliary tip is involved in the construction of the cilium, a hairlike organelle found on most eukaryotic cells. However, the molecular mechanisms of IFT are poorly understood. Here, we found that the two core IFT proteins IFT74 and IFT81 form a tubulin-binding module and mapped the interaction to a calponin homology domain of IFT81 and a highly basic domain in IFT74. Knockdown of IFT81 and rescue experiments with point mutants showed that tubulin binding by IFT81 was required for ciliogenesis in human cells.

The 2.0Å Structure of the Second Calponin Homology Domain from the Actin-binding Region of the Dystrophin Homologue Utrophin

1999 ◽  
Vol 285 (3) ◽  
pp. 1257-1264 ◽  
Author(s):  
Nicholas H. Keep ◽  
Fiona L.M. Norwood ◽  
Carolyn A. Moores ◽  
Steven J. Winder ◽  
John Kendrick-Jones
Keyword(s):  
Actin Binding ◽  
Calponin Homology Domain ◽  
Binding Region ◽  
Calponin Homology

NMR structure of the calponin homology domain of human IQGAP1 and its implications for the actin recognition mode

2010 ◽  
Vol 48 (1) ◽  
pp. 59-64 ◽  
Author(s):  
Ryo Umemoto ◽  
Noritaka Nishida ◽  
Shinji Ogino ◽  
Ichio Shimada
Keyword(s):  
Nmr Structure ◽  
Calponin Homology Domain ◽  
Calponin Homology

Characterization of a novel rice kinesin O12 with a calponin homology domain

2010 ◽  
Vol 149 (1) ◽  
pp. 91-101 ◽  
Author(s):  
N. Umezu ◽  
N. Umeki ◽  
T. Mitsui ◽  
K. Kondo ◽  
S. Maruta
Keyword(s):  
Calponin Homology Domain ◽  
Calponin Homology
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