2013
DOI: 10.1111/gtc.12045
|View full text |Cite
|
Sign up to set email alerts
|

Dab1‐mediated colocalization of multi‐adaptor protein CIN85 with Reelin receptors, ApoER2 and VLDLR, in neurons

Abstract: Reelin-Dab1 signaling is indispensable for proper positioning of neurons in mammalian brain. Reelin is a glycoprotein secreted from Cajal-Reztuis cells in marginal zone of cerebral cortex, and its receptors are Apolipoprotein E receptor 2 (ApoER2) or very low density lipoprotein receptor (VLDLR) expressed on migrating neurons. When Reelin binds to ApoER2 or VLDLR, an adaptor protein Dab1 bound to the receptors undergoes Tyr phosphorylation that is essential for Reelin signaling. We reported previously that Cdk… Show more

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
1
1
1
1

Citation Types

0
8
0

Year Published

2014
2014
2022
2022

Publication Types

Select...
7
2

Relationship

1
8

Authors

Journals

citations
Cited by 12 publications
(9 citation statements)
references
References 55 publications
0
8
0
Order By: Relevance
“…In addition to direct binding of Dab1 to endocytic machinery, there might also be Dab1 interactions with additional co-adaptors that mediate endocytosis of Dab1 cargos. For example, Fuchigami et al demonstrated that Dab1 co-localizes with ApoER2 and CIN85 in vesicle-like structures at the plasma membrane (Fuchigami et al, 2013 ). CIN85 is an adaptor protein involved in endocytosis of receptors including EGFR and dopamine receptor (Dikic, 2003 ; Shimokawa et al, 2010 ) by binding to the cbl-EGFR complex via its SH3 domains and to endophilins via its PRR domain.…”
Section: Other Co-adaptor Proteins For Npxy-motifs Involved In Signalmentioning
confidence: 99%
“…In addition to direct binding of Dab1 to endocytic machinery, there might also be Dab1 interactions with additional co-adaptors that mediate endocytosis of Dab1 cargos. For example, Fuchigami et al demonstrated that Dab1 co-localizes with ApoER2 and CIN85 in vesicle-like structures at the plasma membrane (Fuchigami et al, 2013 ). CIN85 is an adaptor protein involved in endocytosis of receptors including EGFR and dopamine receptor (Dikic, 2003 ; Shimokawa et al, 2010 ) by binding to the cbl-EGFR complex via its SH3 domains and to endophilins via its PRR domain.…”
Section: Other Co-adaptor Proteins For Npxy-motifs Involved In Signalmentioning
confidence: 99%
“…We searched in the human proteome the presence of NPx[Y/F] motifs and found 1823 potential motifs (S0) in 1584 proteins. From these, only 15 proteins (P0) were documented and experimentally tested to have functional unphosphorylated tyrosine-based motifs that interact with PTB-domains (Zhang, 1997; Eigenthaler et al, 1997; Trommsdorff et al, 1998; Dho et al, 1998; Homayouni et al, 1999; Su et al, 2002; Calderwood et al, 2003; Marzolo et al, 2003; Stolt et al, 2003; Zhang et al, 2007; Huang et al, 2009; Park et al, 2010; Barbagallo et al, 2011; Fuchigami et al, 2013). Among them, the NPx[Y/F] motifs of Amyloid-beta precursor protein (APP, UniProtID: P05067), Low-density lipoprotein receptor-related protein 8 (LRP8, UniProtID: Q14114), Krev interaction trapped protein 1 (KRIT1, UniProtID: O00522) have been crystallized with their respective PTB domains present in the X11, GULP1, Dab1, ICAP1 and CCM2 proteins (Stolt et al, 2003; Zhang et al, 2007; Liu and Boggon, 2013; Fisher et al, 2015; Chau et al, 2019).…”
Section: Resultsmentioning
confidence: 99%
“…ApoER2 interacts with different scaffolds and adaptor proteins, such as Dab1, which promotes ApoER2 surface expression, while ligands such as ApoE can promote ApoER2 internalization (Cuitino et al, 2005). Interestingly, the adaptor protein CIN85 binds to Dab1 to potentially mediate internalization of various membrane receptors, including D2R (Shimokawa et al, 2010;Fuchigami et al, 2013). This suggests a possible mechanism for which ApoER2 may be able to influence D2R surface expression.…”
Section: Discussionmentioning
confidence: 99%