On the cover
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.
See pages 553 and 569.
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Nuclear morphology, chromosomal condensation, and transcriptional-mediated localization of genes to the nuclear periphery are disturbed by mutations in cohesin pathway genes.
Pex3p interacts with peroxisome retention factor Inp1p at the peroxisomal membrane and functions in the organelle’s segregation in addition to its biogenesis.
Heparan sulfate glycoproteins dally and dally-like define the germ cell niche in female and male Drosophila, respectively.
FRET analysis of cell lines expressing fluorescently tagged histones on separate nucleosomes demonstrates that variations in chromosome compaction occur during mitosis.
Reevaluation of Lte1’s involvement in the mitotic exit network reveals that it is involved in localizing Bfa1 to the spindle pole body but does not function as a GEF for Tem1.
Spermatogonial stem cells have an innate ability to choose, with constant probability, between different fates independently of cues from the microenvironment.
Adenovirus RID-α activates an autonomous cholesterol regulatory mechanism that rescues defects linked to Niemann-Pick disease type C
Viral subversion of cholesterol homeostasis provides insights into sterol trafficking, autophagy, and lysosomal storage diseases.
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.).