Yeast Ist2 recruits the endoplasmic reticulum to the plasma membrane and creates a ribosome-free membrane microcompartment
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Yeast Ist2 recruits the endoplasmic reticulum to the plasma membrane and creates a ribosome-free membrane microcompartment. / Wolf, Wendelin; Kilic, Annett; Schrul, Bianca; Lorenz, Holger; Schwappach, Blanche; Seedorf, Matthias.
In: PLOS ONE, Vol. 7, No. 7, 2012, p. e39703.Research output: SCORING: Contribution to journal › SCORING: Journal article › Research › peer-review
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TY - JOUR
T1 - Yeast Ist2 recruits the endoplasmic reticulum to the plasma membrane and creates a ribosome-free membrane microcompartment
AU - Wolf, Wendelin
AU - Kilic, Annett
AU - Schrul, Bianca
AU - Lorenz, Holger
AU - Schwappach, Blanche
AU - Seedorf, Matthias
PY - 2012
Y1 - 2012
N2 - The endoplasmic reticulum (ER) forms contacts with the plasma membrane. These contacts are known to function in non-vesicular lipid transport and signaling. Ist2 resides in specific domains of the ER in Saccharomyces cerevisiae where it binds phosphoinositide lipids at the cytosolic face of the plasma membrane. Here, we report that Ist2 recruits domains of the yeast ER to the plasma membrane. Ist2 determines the amount of cortical ER present and the distance between the ER and the plasma membrane. Deletion of IST2 resulted in an increased distance between ER and plasma membrane and allowed access of ribosomes to the space between the two membranes. Cells that overexpress Ist2 showed an association of the nucleus with the plasma membrane. The morphology of the ER and yeast growth were sensitive to the abundance of Ist2. Moreover, Ist2-dependent effects on cytosolic pH and genetic interactions link Ist2 to the activity of the H(+) pump Pma1 in the plasma membrane during cellular adaptation to the growth phase of the culture. Consistently we found a partial colocalization of Ist2-containing cortical ER and Pma1-containing domains of the plasma membrane. Hence Ist2 may be critically positioned in domains that couple functions of the ER and the plasma membrane.
AB - The endoplasmic reticulum (ER) forms contacts with the plasma membrane. These contacts are known to function in non-vesicular lipid transport and signaling. Ist2 resides in specific domains of the ER in Saccharomyces cerevisiae where it binds phosphoinositide lipids at the cytosolic face of the plasma membrane. Here, we report that Ist2 recruits domains of the yeast ER to the plasma membrane. Ist2 determines the amount of cortical ER present and the distance between the ER and the plasma membrane. Deletion of IST2 resulted in an increased distance between ER and plasma membrane and allowed access of ribosomes to the space between the two membranes. Cells that overexpress Ist2 showed an association of the nucleus with the plasma membrane. The morphology of the ER and yeast growth were sensitive to the abundance of Ist2. Moreover, Ist2-dependent effects on cytosolic pH and genetic interactions link Ist2 to the activity of the H(+) pump Pma1 in the plasma membrane during cellular adaptation to the growth phase of the culture. Consistently we found a partial colocalization of Ist2-containing cortical ER and Pma1-containing domains of the plasma membrane. Hence Ist2 may be critically positioned in domains that couple functions of the ER and the plasma membrane.
KW - Cell Membrane/genetics
KW - Cell Nucleus/metabolism
KW - Cytosol/metabolism
KW - Endoplasmic Reticulum/genetics
KW - Gene Expression Regulation, Fungal
KW - Hydrogen-Ion Concentration
KW - Microscopy, Confocal
KW - Microscopy, Fluorescence
KW - Phosphatidylinositols/metabolism
KW - Proton-Translocating ATPases/genetics
KW - Ribosomes/metabolism
KW - Saccharomyces cerevisiae/genetics
KW - Saccharomyces cerevisiae Proteins/genetics
KW - Signal Transduction
U2 - 10.1371/journal.pone.0039703
DO - 10.1371/journal.pone.0039703
M3 - SCORING: Journal article
C2 - 22808051
VL - 7
SP - e39703
JO - PLOS ONE
JF - PLOS ONE
SN - 1932-6203
IS - 7
ER -
