The DOI matches its Crossref record; 5 of the 5 references it cites were found in a registry or an index.
A Role for EHD4 in the Regulation of Early Endosomal Transport
Abstract
All four of the C‐terminal Eps15 homology domain (EHD) proteins have been implicated in the regulation of endocytic trafficking. However, the high level of amino acid sequence identity among these proteins has made it challenging to elucidate the precise function of individual EHD proteins. We demonstrate here with specific peptide antibodies that endogenous EHD4 localizes to Rab5‐, early embryonic antigen 1 (EEA1)‐ and Arf6‐containing endosomes and colocalizes with internalized transferrin in the cell periphery. Knock‐down of EHD4 expression by both small interfering RNA and short hairpin RNA leads to the generation of enlarged early endosomal structures that contain Rab5 and EEA1 as well as internalized transferrin or major histocompatibility complex class I molecules. In addition, cargo destined for degradation, such as internalized low‐density lipoprotein, also accumulates in the enlarged early endosomes in EHD4‐depleted cells. Moreover, we have demonstrated that these enlarged early endosomes are enriched in levels of the activated GTP‐bound Rab5. Finally, we show that endogenous EHD4 and EHD1 interact in cells, suggesting coordinated involvement in the regulation of receptor transport along the early endosome to endocytic recycling compartment axis. The results presented herein provide evidence that EHD4 is involved in the control of trafficking at the early endosome and regulates exit of cargo toward both the recycling compartment and the late endocytic pathway.
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Inactive mutant EHD4G68R shows normal levels of NgCAM endocytosis.
“An inactive mutant of EHD4 (EHD4G68R), on the other hand, which has no ATPase activity, does not bind to membranes, and does not dimerize/oligomerize (Sharma et al., 2008), showed normal levels of NgCAM endocytosis (Fig. 4D).”
From Alterations of EHD1/EHD4 Protein Levels Interfere with L1/NgCAM Endocytosis in Neurons and Disrupt Axonal Targeting (2010) · cites this paper as Sharma et al., 2008
In neurons, EHD4 has been implicated in endocytosis, rather than (or in addition to) recycling.
“In neurons, EHD4 (Shao et al., 2002) has been implicated in endocytosis, rather than (or in addition to) recycling (Sharma et al., 2008).”
From Alterations of EHD1/EHD4 Protein Levels Interfere with L1/NgCAM Endocytosis in Neurons and Disrupt Axonal Targeting (2010) · cites this paper as Sharma et al., 2008
The EHD1V203P mutant shows a significantly decreased capacity for dimerization/oligomerization with EHD family members by co-immunoprecipitation and two-hybrid analysis.
“which shows a significantly decreased capacity for dimerization/oligomerization with EHD family members by co-immunoprecipitation and two-hybrid analysis (Naslavsky et al., 2006; Sharma et al., 2008).”
From Alterations of EHD1/EHD4 Protein Levels Interfere with L1/NgCAM Endocytosis in Neurons and Disrupt Axonal Targeting (2010) · cites this paper as Sharma et al., 2008
The only dimer currently known to exist endogenously is the EHD1/EHD4 dimer.
“Notably, the only dimer currently known to exist endogenously is the EHD1/EHD4 dimer (Sharma et al., 2008).”
From Alterations of EHD1/EHD4 Protein Levels Interfere with L1/NgCAM Endocytosis in Neurons and Disrupt Axonal Targeting (2010) · cites this paper as Sharma et al., 2008
Overexpressed EHD1 strongly interacts with EHD4, and a complex of endogenous EHD1 and EHD4 can be immuno-isolated from cells.
“In keeping with this notion, it has been shown that overexpressed EHD1 strongly interacts with EHD4 and a complex of endogenous EHD1 and EHD4 can be immuno-isolated from cells41.”
From Endocytic recycling protein EHD1 regulates primary cilia morphogenesis and SHH signaling during neural tube development (2016) · cites this paper as [41]
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Metadata
- Authors
- Sharma, M., Naslavsky, N., & Caplan, S.
- Venue
- Traffic
- Publisher
- Wiley
- Published
- 2008-03-06
- Volume
- 9
- Issue
- 6
- Pages
- 995-1018
- ISSN
- 1398-9219
- 1600-0854
- Cited by
- 101
- References
- 5
- Language
- en
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