Intrinsically disordered cytoplasmic domains of two cytokine receptors mediate conserved interactions with membranes
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Intrinsically disordered cytoplasmic domains of two cytokine receptors mediate conserved interactions with membranes. / Haxholm, Gitte Wolfsberg; Nikolajsen, Louise Fletcher; Olsen, Johan Gotthardt; Fredsted, Jacob; Larsen, Flemming Hofmann; Goffin, Vincent; Pedersen, Stine Helene Falsig; Brooks, Andrew J; Waters, Michael J; Kragelund, Birthe Brandt.
I: Biochemical Journal, Bind 468, Nr. 3, 2015, s. 495-506.Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt
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T1 - Intrinsically disordered cytoplasmic domains of two cytokine receptors mediate conserved interactions with membranes
AU - Haxholm, Gitte Wolfsberg
AU - Nikolajsen, Louise Fletcher
AU - Olsen, Johan Gotthardt
AU - Fredsted, Jacob
AU - Larsen, Flemming Hofmann
AU - Goffin, Vincent
AU - Pedersen, Stine Helene Falsig
AU - Brooks, Andrew J
AU - Waters, Michael J
AU - Kragelund, Birthe Brandt
PY - 2015
Y1 - 2015
N2 - Class 1 cytokine receptors regulate essential biological processes through complex intracellular signaling networks. However, the structural platform for understanding their functions is currently incomplete as structure-function studies of the intracellular domains (ICDs) are critically lacking. This study presents the first comprehensive structural characterization of any cytokine receptor ICD and demonstrates that the human prolactin and growth hormone receptor ICDs are intrinsically disordered throughout their entire lengths. We show that they interact specifically with hallmark lipids of the inner plasma membrane leaflet through conserved motifs resembling immuno T-cell receptor activation motifs(ITAMs). However, contrary to the observations made for ITAMs, lipid association of the prolactin and growth hormone receptor ICDs was shown to be unaccompanied by changes in transient secondary structure and independent of tyrosine phosphorylation. The data presented here provides a new structural platform for studying class 1 cytokine receptors and may implicate the membrane as an active component regulating intracellular signaling.
AB - Class 1 cytokine receptors regulate essential biological processes through complex intracellular signaling networks. However, the structural platform for understanding their functions is currently incomplete as structure-function studies of the intracellular domains (ICDs) are critically lacking. This study presents the first comprehensive structural characterization of any cytokine receptor ICD and demonstrates that the human prolactin and growth hormone receptor ICDs are intrinsically disordered throughout their entire lengths. We show that they interact specifically with hallmark lipids of the inner plasma membrane leaflet through conserved motifs resembling immuno T-cell receptor activation motifs(ITAMs). However, contrary to the observations made for ITAMs, lipid association of the prolactin and growth hormone receptor ICDs was shown to be unaccompanied by changes in transient secondary structure and independent of tyrosine phosphorylation. The data presented here provides a new structural platform for studying class 1 cytokine receptors and may implicate the membrane as an active component regulating intracellular signaling.
U2 - 10.1042/BJ20141243
DO - 10.1042/BJ20141243
M3 - Journal article
C2 - 25846210
VL - 468
SP - 495
EP - 506
JO - Biochemical Journal
JF - Biochemical Journal
SN - 0264-6021
IS - 3
ER -
ID: 141044143