SARS-CoV-1 nucleocapsid protein interacts with proteasome subunit p42 (PSMC6). Proteasomes play a central role in the degradation of short-lived and regulatory host proteins. They are also capable of degrading exogenous proteins like viral peptides (Wang et al, 2010).
Homodimers of phosphorylated Stat1, Stat3, and Stat5 and heterodimers of phosphorylated Stat1 and Stat3 translocate from the cytosol to the nucleus (Nicholson et al. 1995, de Koning et al. 1996, Ward et al. 1999, Gits et al. 2006).
Several microRNAs are implicated in posttranscriptional regulation of CDH11 gene expression. The diagram only shows microRNAs reported to downregulate CDH11 mRNA and/or protein levels by at least 2 studies, with at least one study providing human evidence, and at least one study providing mechanistic evidence in the form of luciferase reporter assay and/or formation of the microRNA-mRNA complex. For a more detailed description of criteria for microRNA annotation please refer to Huntely et al. 2016.
The following CDH11-targeting microRNAs are strongly supported by experimental evidence and directly shown in the diagram: miR-200c-3p (Luo et al. 2013; Van der Goten et al. 2014) miR-451a (Yamada et al. 2018; Wang et al. 2020; Wang et al. 2021)
The following microRNAs probably target CDH11, but additional evidence is needed to directly represent them in the diagram: miR-103-2-5p (Gao et al. 2020) miR-127-3p (Dong et al. 2021) miR-148-5p (Kawagoe et al. 2020)
After phosphorylation while bound to phospho-Csf3r at the plasma membrane, p-Stat1,3,5 dissociates from Csf3r prior to dimerizing and transiting to the nucleus (Nicholson et al. 1995, de Koning et al. 1996, Nicholson et al. 1996, Gits et al. 2006).
After phosphorylation by MAP2Ks, a proportion of activated MAPK translocates into the nucleus where it activates nuclear targets (reviewed in Roskoski, 2012b). MAPKs, which lack a nuclear localization signal (NLS), may 'piggyback' into the nucleus in complex with other nuclear-targeted proteins or may translocate by virtue of interaction with components of the nuclear pore complex (Brunet et al, 1999; Adachi et al, 1999; Matsubayashi et al, 2001; Whitehurst et al, 2002; Khokhlatchev et al, 1998; reviewed in Roskoski, 2012b). Although dimerization of MAPKs was thought to be critical for nuclear translocation, a number of studies have now challenged the physiological relevance of MAPK dimerization and this remains an area of uncertainty (Lenormand et al, 1993; Chen et al, 1992; Casar et al, 2008; Lidke et al, 2010; Burack and Shaw, 2005; reviewed in Casar et al, 2009; Roskoski, 2012b)
The kinases Jak2 (Nicholson et al. 1995, Avalos et al. 1997), Tyk2 (Novak et al. 1996, Avalos et al. 1997), Hck (Ward et al. 1998, Santini et al. 2003), and Syk (Corey et al. 1994, Santini et al. 2003) bind phosphorylated tyrosine residues of the cytosolic domain of Csf3r and are activated by phosphorylation.