Molecular Characterization of Two Mitogen-Activated Protein Kinases: p38 MAP Kinase and Ribosomal S6 Kinase From Bombyx mori (Lepidoptera: Bombycidae), and Insight Into Their Roles in Response to BmNPV Infection

Muhammad, Azharuddin; Toufeeq, Shahzad; Yu, Hai-Zhong; Wang, Jie; Zhang, Shang-Zhi; Li, Bing; Li, Zhen; Yang, Li-Ang; Hu, Pei; Ma, Yan; Xu, Jia-Ping

Mitogen-activated protein kinases (MAPKs) are class of evolutionarily conserved protein with Ser/Thr kinase domain. MAPKs have been widely identified from vertebrates to invertebrates, which involve in different signaling transduction pathways (Roux and Blenis 2004) . MAPK family can be classified into three major groups: extracellular signal-regulated kinases (ERKs), C-Jun N-terminal Kinases (JNKs), and p38 MAPKs (Marie Cargnello 2011). In addition, MAPKs are triggered by phosphorylation of conserved TxY motifs present in their Ser/Thr kinase domains. Among them, p38 and ribosomal S6 kinase (S6K) are members of MAPKs play a wide range of functions in various biological processes including apoptosis, pathogen infection, cell differentiation, inflammatory response, UV stress, and environmental stress (Yee et al. 2004 , Regan et al. 2009 , Fenton and Gout 2011 . Both p38 and S6K MAPK homolog have been studied in vertebrates and invertebrates (Han et al. 1998, Fenton and Gout 2011) .