NDLI: Intracellular trafficking of the vacuolar H+-ATPase accessory subunit Ac45.

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Intracellular trafficking of the vacuolar H+-ATPase accessory subunit Ac45.

Content Provider	Semantic Scholar
Author	Jansen, Eric J. R. Holthuis, Joost C. M. McGrouther, C. Burbach, J. Peter H. Martens, G. J.
Copyright Year	1998
Abstract	Ac45 is a type I transmembrane protein associated with vacuolar H+-ATPase, a proton pump mediating the acidification of multiple intracellular organelles. In this study, we examined the intracellular routing of Ac45 in transfected CV-1 fibroblasts. Steady state immunolabeling showed that Ac45 is located on the plasma membrane and in a vacuolar compartment in the juxtanuclear region. Antibody internalization experiments revealed that Ac45 is rapidly retrieved from the cell surface and is targeted to the vacuolar structures. The 26-residue cytoplasmic tail of Ac45 was intrinsically capable of mediating endocytosis of the cell surface protein Tac, indicating that the tail contains an autonomous internalization signal. Immunolocalization studies on cells expressing carboxy-terminally truncated Ac45 mutants showed the presence of essential routing information in the membrane-distal region of the cytoplasmic tail. Further mutational analysis of this region, which lacks the recognized tyrosine- or di-leucine-based sorting motifs, suggested that multiple sites rather than a short linear sequence are responsible for the internalization. Collectively, our results indicate that the cytoplasmic tail of Ac45 contains autonomous targeting information distinct from previously described routing determinants.
Starting Page	2999
Ending Page	3006
Page Count	8
File Format	PDF HTM / HTML
PubMed reference number	9739073
Journal	Medline
Volume Number	111
Part	20
Alternate Webpage(s)	http://jcs.biologists.org/content/joces/111/20/2999.full.pdf
Journal	Journal of cell science
Language	English
Access Restriction	Open
Content Type	Text
Resource Type	Article

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