TY - JOUR
T1 - A model for the role of EHD1-containing membrane tubules in endocytic recycling
AU - Sharma, Mahak
AU - Jovic, Marko
AU - Kieken, Fabien
AU - Naslavsky, Naava
AU - Sorgen, Paul
AU - Caplan, Steve
N1 - Funding Information:
We gratefully acknowledge the support of NIH grants GM074876 and P20 RR018759 (SC), GM072631 (PLS), and the American Heart Association (MS).
PY - 2009
Y1 - 2009
N2 - The C-terminal Eps15 homology domain-containing protein, EHD1, is an important regulator of receptor recycling back to the plasma membrane. In addition to its vesicular localization, EHD1 also localizes to a unique array of tubular membrane structures that emanate from the endocytic recycling compartment. While these structures have been described over seven years ago, addressing their lipid composition and physiological function has been challenging. Moreover, it was not known whether EHD1 itself induces tubule formation, or whether it localizes to pre-existing tubular membrane structures. We have demonstrated that in vivo, EHD1 localizes to pre-existing tubular membranes that contain both phosphatidylinositol-4-phosphate and phosphatidylinositol-(4,5)-bisphosphate. Moreover, we have determined that 'non-tubular' EHD1 mutants with a single residue substitution do not efficiently facilitate receptor recycling. Our data suggest that EHD1-associated tubules are required for efficient recycling and we propose models that describe the potential mechanisms by which EHD1 functions.
AB - The C-terminal Eps15 homology domain-containing protein, EHD1, is an important regulator of receptor recycling back to the plasma membrane. In addition to its vesicular localization, EHD1 also localizes to a unique array of tubular membrane structures that emanate from the endocytic recycling compartment. While these structures have been described over seven years ago, addressing their lipid composition and physiological function has been challenging. Moreover, it was not known whether EHD1 itself induces tubule formation, or whether it localizes to pre-existing tubular membrane structures. We have demonstrated that in vivo, EHD1 localizes to pre-existing tubular membranes that contain both phosphatidylinositol-4-phosphate and phosphatidylinositol-(4,5)-bisphosphate. Moreover, we have determined that 'non-tubular' EHD1 mutants with a single residue substitution do not efficiently facilitate receptor recycling. Our data suggest that EHD1-associated tubules are required for efficient recycling and we propose models that describe the potential mechanisms by which EHD1 functions.
KW - EHD1
KW - Endocytic recycling compartment
KW - Phosphatidylinositol-(4,5)-bisphosphate
KW - Phosphatidylinositol-4-phosphate
KW - Tubules
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U2 - 10.4161/cib.2.5.9157
DO - 10.4161/cib.2.5.9157
M3 - Article
C2 - 19907710
AN - SCOPUS:73849108692
SN - 1942-0889
VL - 2
SP - 431
EP - 433
JO - Communicative and Integrative Biology
JF - Communicative and Integrative Biology
IS - 5
ER -