scholarly journals Plasma Membrane Organization is Poised for Receptor-Mediated Transmembrane Signaling

2021 ◽  
Vol 120 (3) ◽  
pp. 94a-95a
Author(s):  
Nirmalya Bag ◽  
David A. Holowka ◽  
Barbara A. Baird
2020 ◽  
Vol 118 (3) ◽  
pp. 247a
Author(s):  
Nirmalya Bag ◽  
David A. Holowka ◽  
Barbara A. Baird

2012 ◽  
Vol 287 (8) ◽  
pp. 607-620 ◽  
Author(s):  
Agustina Olivera-Couto ◽  
Pablo S. Aguilar

Development ◽  
1991 ◽  
Vol 111 (4) ◽  
pp. 1021-1028 ◽  
Author(s):  
C. Hashimoto ◽  
S. Gerttula ◽  
K.V. Anderson

Formation of the Drosophila embryo's dorsal-ventral pattern requires the maternal product of the Toll gene. DNA sequence and genetic analyses together suggested that the Toll gene product is a transmembrane protein which communicates information from an extracytoplasmic compartment to the cytoplasm. Using antibodies as probes, we show that the Toll protein is a 135 × 10(3) Mr glycoprotein which is tightly associated with embryonic membranes. During the syncytial stage when dorsal-ventral polarity is established, the maternal Toll protein is associated with the plasma membrane around the entire embryo. During later embryonic stages, the Toll protein is expressed zygotically on many cell surfaces, possibly to promote cell adhesion. The plasma membrane localization of the Toll protein in the syncytial embryo suggests that transmembrane signaling from the extracellular perivitelline space to the cytoplasm is required for establishment of the embryonic dorsal-ventral pattern.


2009 ◽  
Vol 185 (6) ◽  
pp. 959-967 ◽  
Author(s):  
Takashi Ishiuchi ◽  
Kazuyo Misaki ◽  
Shigenobu Yonemura ◽  
Masatoshi Takeichi ◽  
Takuji Tanoue

Compartmentalization of the plasma membrane in a cell is fundamental for its proper functions. In this study, we present evidence that mammalian Fat4 and Dachsous1 cadherins regulate the apical plasma membrane organization in the embryonic cerebral cortex. In neural progenitor cells of the cortex, Fat4 and Dachsous1 were concentrated together in a cell–cell contact area positioned more apically than the adherens junction (AJ). These molecules interacted in a heterophilic fashion, affecting their respective protein levels. We further found that Fat4 associated and colocalized with the Pals1 complex. Ultrastructurally, the apical junctions of the progenitor cells comprised the AJ and a stretch of plasma membrane apposition extending apically from the AJ, which positionally corresponded to the Fat4–Dachsous1-positive zone. Depletion of Fat4 or Pals1 abolished this membrane apposition. These results highlight the importance of the Fat4–Dachsous1–Pals1 complex in organizing the apical membrane architecture of neural progenitor cells.


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