Biochemical and Biophysical Research Communications
Regular ArticleMolecular Cloning of p125Nap1, a Protein That Associates with an SH3 Domain of Nck
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Cited by (58)
WASP family proteins: Molecular mechanisms and implications in human disease
2022, European Journal of Cell BiologyWASp family verprolin-homologous protein-2 (WAVE2) and Wiskott-Aldrich Syndrome Protein (WASp) engage in distinct downstream signaling interactions at the T cell antigen receptor site
2014, Journal of Biological ChemistryCitation Excerpt :The interaction of WAVE2 and Nck can be mediated by a direct interaction of the PRD of WAVE2 with one of the SH3 domains of Nck or indirectly through Hem1, a WAVE2-associated protein. Hem1 interacts with the N terminus SH3 domain of Nck (51) and, therefore, might mediate an indirect interaction between Nck and WAVE2 WHD. To identify the molecular link between Nck and WAVE2 and to determine potential competition with WASp, we investigated which of the proposed interactions occurs.
Activation of the WAVE Complex by Coincident Signals Controls Actin Assembly
2009, Molecular CellCitation Excerpt :However, in cells, WAVE proteins are found as a complex (the WAVE complex) with four other proteins: Pir121, Nap 1, Abi-1, and HSPC300 or their homologs (Eden et al., 2002; Gautreau et al., 2004). Importantly, Pir121 and its homolog Sra-1 can bind activated Rac (Kobayashi et al., 1998), and Nap 1 can bind the SH3 domain of the adaptor protein Nck (Kitamura et al., 1996). Although it is clear that the WAVE complex plays an important regulatory role, its biochemical characterization has been difficult and contentious.
Nap1-Regulated Neuronal Cytoskeletal Dynamics Is Essential for the Final Differentiation of Neurons in Cerebral Cortex
2007, NeuronCitation Excerpt :Nap1 is a member of the WAVE complex. Nap1, which interacts directly with Sra1/PIR121 (which binds to GTP-bound Rac1) and Abi1 (which binds the SH3 domain of Nck), forms a tetrameric complex containing Sra1/PIR121, Abi1/2, and HSPC300 to regulate WAVE1 activity (Kitamura et al., 1996, 1997; Kobayashi et al., 1998; Hummel et al., 2000; Soto et al., 2002; Yamamoto et al., 2001; Eden et al., 2002). WAVE1, in contrast to the related WASP proteins, which are autoinhibitory and are activated by binding GTP-bound Cdc42 to participate in the formation of filopodia, is constitutively active and acts downstream of Rac1 to initiate lamellipodia formation (Biyasheva et al., 2004; Blagg and Insall, 2004; Cory and Ridley, 2002; Machesky et al., 1999; Miki et al., 1998; Nakagawa et al., 2001; Innocenti et al., 2004; Kunda et al., 2003; Rogers et al., 2003; Rohatgi et al., 2000; Steffen et al., 2004).
Protein complexes regulating Arp2/3-mediated actin assembly
2006, Current Opinion in Cell BiologyArabidopsis GNARLED encodes a NAP125 homolog that positively regulates ARP2/3
2004, Current Biology
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The first two authors contributed equally to this work.
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Present address: Cardiovascular Research Center, Massachusetts General Hospital-East, and Department of Medicine, Harvard Medical School, Charlestown, MA 02129.
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To whom correspondence may be addressed. M.K. fax: 81-78-382-2080; K.Y. fax: 617-726-5806.