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Molecular electron tomography reveals that the extracellular domain of the homophilic cell adhesion molecule CEACAM1 adopts a variety of conformations. Adhesion-induced rearrangements in the protein's self-association alters downstream, cytoplasmic signaling pathways.
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How cell adhesion molecules transmit signals across the plasma membrane.
People & Ideas
Michael Buszczak: Tracking the big game in stem cell identity
Buszczak is exploring the regulation of proteins that control stem cell identity in the fly.
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Lte1 contributes to Bfa1 localization rather than stimulating nucleotide exchange by Tem1
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Membrane expansion alleviates endoplasmic reticulum stress independently of the unfolded protein response
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Adenovirus RID-α activates an autonomous cholesterol regulatory mechanism that rescues defects linked to Niemann-Pick disease type C
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The CEACAM1 N-terminal Ig domain mediates cis- and trans-binding and is essential for allosteric rearrangements of CEACAM1 microclusters
Structural analyses reveal that oligomerization between cell adhesion molecules in the same membrane is influenced by their interactions across opposing membranes (see also in this issue the accompanying paper by Müller et al.).
Homophilic adhesion and CEACAM1-S regulate dimerization of CEACAM1-L and recruitment of SHP-2 and c-Src
The monomer/dimer equilibrium of adhesion molecule CEACAM1-L is regulated by binding between opposing membranes, which in turn controls cytoplasmic enzyme binding and signaling (see also in this issue the accompanying paper by Klaile et al.).
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