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Vol. 12, Issue 11, 3465-3475, November 2001
and
§
*Department of Cell Biology and Neuroscience and
Cellular junctions are critical for intercellular communication and
for the assembly of cells into tissues. Cell junctions often consist of
tight junctions, which form a permeability barrier and prevent the
diffusion of lipids and proteins between cell compartments, and
adherens junctions, which control the adhesion of cells and link
cortical actin filaments to attachment sites on the plasma membrane.
Proper tight junction formation and cell polarity require the function
of membrane-associated guanylate kinases (MAGUKs) that contain the PDZ
protein-protein interaction domain. In contrast, less is known about
how adherens junctions are assembled. Here we describe how the
PDZ-containing protein DLG-1 is required for the proper formation and
function of adherens junctions in Caenorhabditis
elegans. DLG-1 is a MAGUK protein that is most similar in
sequence to mammalian SAP97, which is found at both synapses of the
CNS, as well as at cell junctions of epithelia. DLG-1 is localized to
adherens junctions, and DLG-1 localization is mediated by an
amino-terminal domain shared with SAP97 but not found in other MAGUK
family members. DLG-1 recruits other proteins and signaling molecules
to adherens junctions, while embryos that lack DLG-1 fail to recruit
the proteins AJM-1 and CPI-1 to adherens junctions. DLG-1 is required
for the proper organization of the actin cytoskeleton and for the
morphological elongation of embryos. In contrast to other proteins that
have been observed to affect adherens junction assembly and function, DLG-1 is not required to maintain cell polarity. Our results suggest a
new function for MAGUK proteins distinct from their role in cell polarity.
The Waksman Institute, Department of Genetics, Rutgers
University, Piscataway, NJ 08854
Corresponding author. E-mail address:
rongo{at}waksman.rutgers.edu
§
Both authors contributed equally to this work.
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