منابع مشابه
PAR proteins cross the boundary
L ike Berlin during the Cold War, the membrane of a single-celled C. elegans embryo is divided. But unlike Berlin, no barrier separates the two sections, Goehring et al. conclude (1) after discovering that PAR proteins can travel freely between the anterior and posterior domains of the membrane. The researchers tested several explanations for what preserves the difference between these domains ...
متن کاملPAR proteins diffuse freely across the anterior–posterior boundary in polarized C. elegans embryos
Polarization of cells by PAR proteins requires the segregation of antagonistic sets of proteins into two mutually exclusive membrane-associated domains. Understanding how nanometer scale interactions between individual PAR proteins allow spatial organization across cellular length scales requires determining the kinetic properties of PAR proteins and how they are modified in space. We find that...
متن کاملElaborating polarity: PAR proteins and the cytoskeleton.
Cell polarity is essential for cells to divide asymmetrically, form spatially restricted subcellular structures and participate in three-dimensional multicellular organization. PAR proteins are conserved polarity regulators that function by generating cortical landmarks that establish dynamic asymmetries in the distribution of effector proteins. Here, we review recent findings on the role of PA...
متن کاملPar Proteins: Partners in Polarization
Proteins can be localized either by inclusion or exclusion, and the Par polarity proteins illustrate both mechanisms. Cdc42 recruits Par-6 to a limited region of the plasma membrane. Par-6 recruits Par-3, which is actively removed from other regions by Par-1 and Par-5. Inclusion and exclusion together ensure efficient segregation of the polarity proteins.
متن کاملCell polarity: Scaffold proteins par excellence
Par proteins are involved in determining cellular asymmetry. Recent studies have identified one of these proteins, Par6, as a key regulator of cell polarity and transformation via its interactions with small GTPases and atypical forms of protein kinase C.
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ژورنال
عنوان ژورنال: Journal of Cell Biology
سال: 2011
ISSN: 1540-8140,0021-9525
DOI: 10.1083/jcb.1933if