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Singhvi, A, Teuliere, J, Talavera, K, Cordes, S, Ou, G, Vale, RD, Prasad, BC, Clark, SG and Garriga, G (2011) The Arf GAP CNT-2 regulates the apoptotic fate in C. elegans asymmetric neuroblast divisions. Curr. Biol. 21:948-54


During development, all cells make the decision to live or die. Although the molecular mechanisms that execute the apoptotic program are well defined, less is known about how cells decide whether to live or die. In C. elegans, this decision is linked to how cells divide asymmetrically [1, 2]. Several classes of molecules are known to regulate asymmetric cell divisions in metazoans, yet these molecules do not appear to control C. elegans divisions that produce apoptotic cells [3]. We identified CNT-2, an Arf GTPase-activating protein (GAP) of the AGAP family, as a novel regulator of this type of neuroblast division. Loss of CNT-2 alters daughter cell size and causes the apoptotic cell to adopt the fate of its sister cell, resulting in extra neurons. CNT-2's Arf GAP activity is essential for its function in these divisions. The N terminus of CNT-2, which contains a GTPase-like domain that defines the AGAP class of Arf GAPs, negatively regulates CNT-2's function. We provide evidence that CNT-2 regulates receptor-mediated endocytosis and consider the implications of its role in asymmetric cell divisions.


PubMed PMC3109113 Online version:10.1016/j.cub.2011.04.025


ADP-Ribosylation Factor 1/physiology; ADP-Ribosylation Factors/physiology; Animals; Apoptosis; Caenorhabditis elegans/cytology; Caenorhabditis elegans/genetics; Caenorhabditis elegans/metabolism; Caenorhabditis elegans Proteins/genetics; Caenorhabditis elegans Proteins/metabolism; Caenorhabditis elegans Proteins/physiology; Cell Division/physiology; Cell Polarity; Endocytosis/genetics; GTPase-Activating Proteins/genetics; GTPase-Activating Proteins/metabolism; GTPase-Activating Proteins/physiology