2010
DOI: 10.1016/j.bbrc.2010.09.133
|View full text |Cite
|
Sign up to set email alerts
|

SID1 transmembrane family, member 2 (Sidt2): A novel lysosomal membrane protein

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
3
1
1

Citation Types

7
57
0

Year Published

2012
2012
2017
2017

Publication Types

Select...
9

Relationship

0
9

Authors

Journals

citations
Cited by 55 publications
(64 citation statements)
references
References 24 publications
7
57
0
Order By: Relevance
“…In contrast, minimal co-localisation was observed between SIDT2 and EEA1 (Pearson’s r = 0.25) (Figure 1A, Supplemental video 3 and 4) or RAB11 (Pearson’s r = 0.06) (data not shown), which demarcate early and recycling endosomes respectively. These data indicate that SIDT2 predominantly resides in late endosomes and lysosomes, and are consistent with previous reports localising endogenously-expressed SIDT2 to the endo-lysosomal compartment (Buschow et al, 2012; Gao et al, 2010). …”
Section: Resultssupporting
confidence: 93%
“…In contrast, minimal co-localisation was observed between SIDT2 and EEA1 (Pearson’s r = 0.25) (Figure 1A, Supplemental video 3 and 4) or RAB11 (Pearson’s r = 0.06) (data not shown), which demarcate early and recycling endosomes respectively. These data indicate that SIDT2 predominantly resides in late endosomes and lysosomes, and are consistent with previous reports localising endogenously-expressed SIDT2 to the endo-lysosomal compartment (Buschow et al, 2012; Gao et al, 2010). …”
Section: Resultssupporting
confidence: 93%
“…Although mammals have sophisticated immune systems and long dsRNA induces innate immune responses in mammalian cells, recent studies show that long dsRNA-mediated RNA interference exists and functions as an antiviral mechanism in mammals (31,32). M. musculus and Rattus norvegicus endogenously express SIDT2, which is an integral membrane protein that is primarily localized in the lysosome (33). Lysosomal SIDT2 may recognize dsRNA that localizes in the endocytic pathway.…”
Section: Discussionmentioning
confidence: 99%
“…In planaria, silencing in response to ingested dsRNA can occur in most tissues (Rouhana et al, 2013) and weak homologs of SID-1 are present (Zayas et al, 2005) but the roles of these homologs in the uptake of dsRNA are yet to be evaluated. Finally, a mammalian homolog of SID-1, SidT2, is a lysosomal membrane protein (Jialin et al, 2010), which is in contrast to the reported plasma membrane localization of C. elegans SID-1 (Winston et al, 2002), and mouse knockouts of SidT2 have impaired glucose tolerance (Gao et al, 2013), which is in contrast to the lack of obvious defects in C. elegans that lack SID-1 (Winston et al, 2002), suggesting that SID-1 and its mammalian homologs also have alternative function(s). An intriguing clue to such alternative functions comes from a close inspection of sequence similarity, which suggests that both SID-1 and CHUP-1 have a domain with weak similarity to hydrolases (Pei et al, 2011).…”
Section: Import Into Cellsmentioning
confidence: 99%