Our previous study found that the nuclear protein, 68-kDa Src-associated in 
mitosis protein (Sam68), is translocated to the cytoplasm and forms punctate 
pattern during enterovirus 71 (EV71) infection [Virus Research, 180 (2014), 
1-11]. However, the exact function of this punctate pattern in cytoplasm during 
EV71 infection remains unknown. In this study, we firstly have examined this 
punctate pattern of Sam68 re-localization in the cytoplasm, and observed the 
obvious recruitments of Sam68 to the EV71-induced stress granules (SGs). Sam68, 
belongs to the KH domain family of RNA binding proteins (RBPs), was then 
confirmed that its KH domain was essential for this recruitment. Nevertheless, 
Knockdown of Sam68 expression using ShRNA had no effects on SGs assembly, 
indicating that Sam68 is not a constitutive component of the SGs during EV71 
infection. Lastly, we investigated the importance of microtubulin transport to 
SGs aggregation, and revealed that microtubule depolymerization inhibited SGs 
formation, suggesting that EV71-induced SGs move throughout the cytoplasm in a 
microtubule-dependent manner. Taken together, these results illuminated that 
EV71 infections can induce SGs formation, and Sam68, as a SGs component, 
migrates alone with SGs dependent on intact microtubule upon the viral 
infections. These findings may provide novel underlying mechanism for 
delineating the role of SGs during EV71 infection.