NDLI: Transport of LAPTM5 to lysosomes requires association with the ubiquitin ligase Nedd4, but not LAPTM5 ubiquitination

Content Provider	PubMed Central
Author	Pak, Youngshil Glowacka, Wioletta K. Bruce, M. Christine Pham, Nam Rotin, Daniela
Copyright Year	2006
Abstract	LAPTM5 is a lysosomal transmembrane protein expressed in immune cells. We show that LAPTM5 binds the ubiquitin-ligase Nedd4 and GGA3 to promote LAPTM5 sorting from the Golgi to the lysosome, an event that is independent of LAPTM5 ubiquitination. LAPTM5 contains three PY motifs (L/PPxY), which bind Nedd4-WW domains, and a ubiquitin-interacting motif (UIM) motif. The Nedd4–LAPTM5 complex recruits ubiquitinated GGA3, which binds the LAPTM5-UIM; this interaction does not require the GGA3-GAT domain. LAPTM5 mutated in its Nedd4-binding sites (PY motifs) or its UIM is retained in the Golgi, as is LAPTM5 expressed in cells in which Nedd4 or GGA3 is knocked-down with RNAi. However, ubiquitination-impaired LAPTM5 can still traffic to the lysosome, suggesting that Nedd4 binding to LAPTM5, not LAPTM5 ubiquitination, is required for targeting. Interestingly, Nedd4 is also able to ubiquitinate GGA3. These results demonstrate a novel mechanism by which the ubiquitin-ligase Nedd4, via interactions with GGA3 and cargo (LAPTM5), regulates cargo trafficking to the lysosome without requiring cargo ubiquitination.
Related Links	http://dx.doi.org/10.1083/jcb.200603001
Ending Page	645
Page Count	15
Starting Page	631
File Format	PDF
ISSN	00219525
e-ISSN	15408140
Journal	The Journal of Cell Biology
Issue Number	4
Volume Number	175
Language	English
Publisher	The Rockefeller University Press
Publisher Date	2006-11-20
Access Restriction	Open
Rights Holder	The Rockefeller University Press
Subject Keyword	Cell Biology Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Cell Biology Medicine

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