Ubiquitin is attached to membranes of baculovirus particles by a novel type of phospholipid anchor
Article Abstract:
Free ubiquitin, present in large quantities in purified budded virions of Autographa Californica nuclear polyhedrosis virus (AcNPV), differs from standard ubiquitin in its electrophoretic mobility on SDS gels. Phase extraction studies indicate the modified form of ubiquitin to be an integral membrane protein. Phopholipase treatment alters the electrophoretic mobility of the phosphate- and palmitate-labeled membrane-bound form of ubiquitin, indicating that a new phospholipid type anchor binds ubiquitin to the inner face of the viral membrane.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 1995
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Clustering membrane proteins: it's all coming together with the PSD-95/SAP90 protein family
Article Abstract:
The clustering of membrane proteins in the neurons may be mediated by the action of PSD-95/SAP90 proteins. These proteins are abundant in neuronal membranes and are found typically associated with ion channels. This family of proteins can be identified by the presence of PDZ domains in their structures and are similar to the neuronal nitric oxide synthase membrane protein. Their function is attributed to their ability to bind NMDA receptors and Shaker-types subunits.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 1996
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The RCK domain of the KtrAB [K.sup.+] transporter: Multiple conformations of an octameric ring
Article Abstract:
The experimental evidence to show the association between one regulating the conductance of [K.sup.+] (RCK) octameric ring and two KtrB membrane proteins are presented. The findings reveal that the RCK domains of the KtrAB transporter and MthK channel share the same fold, have partially overlapping ligand sites, and form octameric rings with similar up-and-down architecture.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 2006
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