TY - JOUR
T1 - Localization and structure of the ankyrin-binding site on β 2-spectrin
AU - Davis, Lydia
AU - Abdi, Khadar
AU - Machius, Mischa
AU - Brautigam, Chad A
AU - Tomchick, Diana R
AU - Bennett, Vann
AU - Michaely, Peter A
PY - 2009/3/13
Y1 - 2009/3/13
N2 - Spectrins are tetrameric actin-cross-linking proteins that form an elastic network, termed the membrane skeleton, on the cytoplasmic surface of cellular membranes. At the plasma membrane, the membrane skeleton provides essential support, preventing loss of membrane material to environmental shear stresses. The skeleton also controls the location, abundance, and activity of membrane proteins that are critical to cell and tissue function. The ability of the skeleton to modulate membrane stability and function requires adaptor proteins that bind the skeleton to membranes. The principal adaptors are the ankyrin proteins, which bind to the β-subunit of spectrin and to the cytoplasmic domains of numerous integral membrane proteins. Here, we present the crystal structure of the ankyrin-binding domain of human β 2-spectrin at 1.95 Å resolution together with mutagenesis data identifying the binding surface for ankyrins on β 2-spectrin.
AB - Spectrins are tetrameric actin-cross-linking proteins that form an elastic network, termed the membrane skeleton, on the cytoplasmic surface of cellular membranes. At the plasma membrane, the membrane skeleton provides essential support, preventing loss of membrane material to environmental shear stresses. The skeleton also controls the location, abundance, and activity of membrane proteins that are critical to cell and tissue function. The ability of the skeleton to modulate membrane stability and function requires adaptor proteins that bind the skeleton to membranes. The principal adaptors are the ankyrin proteins, which bind to the β-subunit of spectrin and to the cytoplasmic domains of numerous integral membrane proteins. Here, we present the crystal structure of the ankyrin-binding domain of human β 2-spectrin at 1.95 Å resolution together with mutagenesis data identifying the binding surface for ankyrins on β 2-spectrin.
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U2 - 10.1074/jbc.M809245200
DO - 10.1074/jbc.M809245200
M3 - Article
C2 - 19098307
AN - SCOPUS:65449178092
SN - 0021-9258
VL - 284
SP - 6982
EP - 6987
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
IS - 11
ER -