TY - JOUR
T1 - A novel 4.1 ezrin radixin moesin (FERM)-containing protein, 'Willin'
AU - Gunn-Moore, Frank J.
AU - Welsh, Gavin I.
AU - Herron, Lissa R.
AU - Brannigan, Frances
AU - Venkateswarlu, Kanamarlapudi
AU - Gillespie, Stewart
AU - Brandwein-Gensler, Margaret
AU - Madan, Rashna
AU - Tavaré, Jeremy M.
AU - Brophy, Peter J.
AU - Prystowsky, Michael B.
AU - Guild, Simon
N1 - Funding Information:
We thank the BBSRC for funding to FJGM; MRC program grant funding to J.M.T.; the Maitland-Ramsay PhD fellowship to L.R.H. We also are grateful to Dr. T. Vaughan (University of St. Andrews) for help in obtaining static images and Dr. V. Zaitsev (University of St Andrews) for help in the alignment program.
PY - 2005/9/12
Y1 - 2005/9/12
N2 - The 4.1 superfamily of proteins contain a 4.1 Ezrin Radixin Moesin (FERM) domain and are described as linking the cytoskeleton with the plasma membrane. Here, we describe a new FERM domain-containing protein called Willin. Willin has a recognizable FERM domain within its N-terminus and is capable of binding phospholipids. Its intra-cellular distribution can be cytoplasmic or at the plasma membrane where it can co-localize with actin. However, the plasma membrane location of Willin is not influenced by cytochalasin D induced actin disruption but it is induced by the addition of epidermal growth factor.
AB - The 4.1 superfamily of proteins contain a 4.1 Ezrin Radixin Moesin (FERM) domain and are described as linking the cytoskeleton with the plasma membrane. Here, we describe a new FERM domain-containing protein called Willin. Willin has a recognizable FERM domain within its N-terminus and is capable of binding phospholipids. Its intra-cellular distribution can be cytoplasmic or at the plasma membrane where it can co-localize with actin. However, the plasma membrane location of Willin is not influenced by cytochalasin D induced actin disruption but it is induced by the addition of epidermal growth factor.
KW - 4.1 ezrin radixin moesin
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U2 - 10.1016/j.febslet.2005.07.097
DO - 10.1016/j.febslet.2005.07.097
M3 - Article
C2 - 16137681
AN - SCOPUS:24144443452
SN - 0014-5793
VL - 579
SP - 5089
EP - 5094
JO - FEBS Letters
JF - FEBS Letters
IS - 22
ER -