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2.
Nature ; 543(7645): 327, 2017 03 15.
Article in English | MEDLINE | ID: mdl-28300111
3.
Nature ; 537(7620): 319, 2016 09 15.
Article in English | MEDLINE | ID: mdl-27629637
5.
7.
Nature ; 505(7483): 301, 2014 Jan 16.
Article in English | MEDLINE | ID: mdl-24429627

Subject(s)
Biology , Biology/trends
9.
Nature ; 480(7378): 463, 2011 Dec 21.
Article in English | MEDLINE | ID: mdl-22193097
11.
Nature ; 475(7356): 307, 2011 Jul 20.
Article in English | MEDLINE | ID: mdl-21776075
12.
Nature ; 467(7315): 539, 2010 Sep 30.
Article in English | MEDLINE | ID: mdl-20882004
18.
Traffic ; 9(10): 1743-56, 2008 Sep.
Article in English | MEDLINE | ID: mdl-18636990

ABSTRACT

Of many lipid transfer proteins identified, all have been implicated in essential cellular processes, but the activity of none has been demonstrated in intact cells. Among these, phosphatidylinositol transfer proteins (PITP) are of particular interest as they can bind to and transfer phosphatidylinositol (PtdIns)--the precursor of important signalling molecules, phosphoinositides--and because they have essential functions in neuronal development (PITPalpha) and cytokinesis (PITPbeta). Structural analysis indicates that, in the cytosol, PITPs are in a 'closed' conformation completely shielding the lipid within them. But during lipid exchange at the membrane, they must transiently 'open'. To study PITP dynamics in intact cells, we chemically targeted their C95 residue that, although non-essential for lipid transfer, is buried within the phospholipid-binding cavity, and so, its chemical modification prevents PtdIns binding because of steric hindrance. This treatment resulted in entrapment of open conformation PITPs at the membrane and inactivation of the cytosolic pool of PITPs within few minutes. PITP isoforms were differentially inactivated with the dynamics of PITPbeta faster than PITPalpha. We identify two tryptophan residues essential for membrane docking of PITPs.


Subject(s)
Cell Membrane , Phosphatidylinositols/metabolism , Phospholipid Transfer Proteins/metabolism , 2,2'-Dipyridyl/analogs & derivatives , 2,2'-Dipyridyl/pharmacology , Animals , Binding Sites , COS Cells , Cell Membrane/drug effects , Cell Membrane/metabolism , Chlorocebus aethiops , Cytosol/drug effects , Cytosol/metabolism , Disulfides/pharmacology , Endoplasmic Reticulum/drug effects , Endoplasmic Reticulum/metabolism , Escherichia coli/genetics , Ethylmaleimide/pharmacology , Golgi Apparatus/drug effects , Golgi Apparatus/metabolism , HL-60 Cells , Humans , Models, Molecular , Mutation , PC12 Cells , Phosphatidylinositols/chemistry , Phospholipid Transfer Proteins/chemistry , Phospholipid Transfer Proteins/genetics , Protein Binding , Protein Transport , Rats , Transfection , Tryptophan/metabolism
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