Interaction of ALG-2 with ASK1 influences ASK1 localization and subsequent JNK activation.
ALG-2 (apoptosis linked gene-2) is an essential protein for the execution of apoptosis whose function is largely unknown. Here, we demonstrate that ALG-2 could interact with the C-terminus (amino acids 941-1375) of the apoptosis signal-regulating kinase 1 (ASK1) in BOSC23 cells as well as in vitro. ASK1 failed to bind to an isotype of ALG-2 found in the liver, ALG-2,1, in which two amino acids (Gly-121 and Phe-122) are deleted. This implies that the interaction is very specific. Cotransfection with ALG-2 resulted in the nuclear presence of ASK1 and inhibited the activation of c-Jun N-terminal kinase (JNK) by ASK1 in BOSC23 cells. This study reports that ALG-2 could regulate the subcellular localization and the JNK activity modulation of ASK1 by direct interaction.
Hwang
In-Sik
IS
Research Center for Biomedicinal Resources and Division of Life Science, PaiChai University, 439-6 Doma-2-dong, Seo-gu, Taejon 302-735, South Korea.
Jung
Yong-Sam
YS
Kim
Eunhee
E
D002460:Cell Line; D002467:Cell Nucleus / Q000201:enzymology; D004789:Enzyme Activation; D005455:Fluorescent Antibody Technique; D048031:JNK Mitogen-Activated Protein Kinases; D048848:MAP Kinase Kinase Kinase 5; D020930:MAP Kinase Kinase Kinases / Q000378:metabolism*; D020928:Mitogen-Activated Protein Kinases / Q000378:metabolism*; D011485:Protein Binding
D048031:JNK Mitogen-Activated Protein Kinases; D020928:Mitogen-Activated Protein Kinases; D048848:MAP Kinase Kinase Kinase 5; D020930:MAP Kinase Kinase Kinases