Retention of p63 in an ER-Golgi intermediate compartment depends on the presence of all three of its domains and on its ability to form oligomers

doi:10.1083/jcb.126.1.25

This Article

	Full Text (PDF, 4790K)
	Alert me when this article is cited
	Citation Map

Services

	Email this article
	Similar articles in this journal
	Similar articles in PubMed
	Alert me to new content in the JCB
	Download to citation manager

Citing Articles

	Citing Articles via HighWire
	Citing Articles via CrossRef
	Citing Articles via Google Scholar

Google Scholar

	Articles by Schweizer, A.
	Articles by Kornfeld, S.
	Search for Related Content

PubMed

	PubMed Citation
	Articles by Schweizer, A.
	Articles by Kornfeld, S.

Social Bookmarking

	What's this?

ARTICLES

Retention of p63 in an ER-Golgi intermediate compartment depends on the presence of all three of its domains and on its ability to form oligomers

A Schweizer, J Rohrer, HP Hauri and S Kornfeld
Department of Medicine, Washington University School of Medicine, St. Louis, Missouri 63110.

The type II membrane protein p63 is a resident protein of a membrane network interposed between rough ER and Golgi apparatus. To study the retention of p63, mutant forms were expressed in COS cells and the intracellular distribution determined by immunofluorescence microscopy. Investigation of chimeric constructs between p63 and the plasma membrane protein dipeptidylpeptidase IV showed that protein sequences from all three domains of the p63 protein are required to achieve complete intracellular retention. Mutational analysis of the 106-amino acid cytoplasmic tail of p63 revealed that the NH2-terminal 23 amino acids are necessary for retention. When p63 was solubilized with Triton X-100 and subjected to centrifugation at 100,000 g, it formed large, insoluble oligomers, particularly at neutral pH and below. A comparison of the behavior of wildtype and mutant p63 proteins in this assay revealed a perfect correlation between the formation of large oligomers and correct intracellular retention. These results suggest that self- association may be a major mechanism by which p63 is retained between the rough ER and the Golgi apparatus.
Add to CiteULike CiteULike Add to Complore Complore Add to Connotea Connotea Add to Del.icio.us Del.icio.us Add to Digg Digg Facebook Add to Reddit Reddit Add to Technorati Technorati Twitter What's this?

This article has been cited by other articles:

Planey, S. L., Keay, S. K., Zhang, C.-O., Zacharias, D. A. (2009). Palmitoylation of Cytoskeleton Associated Protein 4 by DHHC2 Regulates Antiproliferative Factor-mediated Signaling. Mol. Biol. Cell 20: 1454-1463 [Abstract] [Full Text]
Schaecher, S. R., Diamond, M. S., Pekosz, A. (2008). The Transmembrane Domain of the Severe Acute Respiratory Syndrome Coronavirus ORF7b Protein Is Necessary and Sufficient for Its Retention in the Golgi Complex. J. Virol. 82: 9477-9491 [Abstract] [Full Text]
Zhang, J., Planey, S. L., Ceballos, C., Stevens, S. M. Jr., Keay, S. K., Zacharias, D. A. (2008). Identification of CKAP4/p63 as a Major Substrate of the Palmitoyl Acyltransferase DHHC2, a Putative Tumor Suppressor, Using a Novel Proteomics Method. Mol. Cell. Proteomics 7: 1378-1388 [Abstract] [Full Text]
Gupta, N., Manevich, Y., Kazi, A. S., Tao, J.-Q., Fisher, A. B., Bates, S. R. (2006). Identification and characterization of p63 (CKAP4/ERGIC-63/CLIMP-63), a surfactant protein A binding protein, on type II pneumocytes. Am. J. Physiol. Lung Cell. Mol. Physiol. 291: L436-L446 [Abstract] [Full Text]
Vedrenne, C., Klopfenstein, D. R., Hauri, H.-P. (2005). Phosphorylation Controls CLIMP-63-mediated Anchoring of the Endoplasmic Reticulum to Microtubules. Mol. Biol. Cell 16: 1928-1937 [Abstract] [Full Text]
Fenteany, F. H., Colley, K. J. (2005). Multiple Signals Are Required for {alpha}2,6-Sialyltransferase (ST6Gal I) Oligomerization and Golgi Localization. J. Biol. Chem. 280: 5423-5429 [Abstract] [Full Text]
Parker, A. K. T., Gergely, F. V., Taylor, C. W. (2004). Targeting of Inositol 1,4,5-Trisphosphate Receptors to the Endoplasmic Reticulum by Multiple Signals within Their Transmembrane Domains. J. Biol. Chem. 279: 23797-23805 [Abstract] [Full Text]
Pottekat, A., Menon, A. K. (2004). Subcellular Localization and Targeting of N-Acetylglucosaminyl Phosphatidylinositol De-N-acetylase, the Second Enzyme in the Glycosylphosphatidylinositol Biosynthetic Pathway. J. Biol. Chem. 279: 15743-15751 [Abstract] [Full Text]
Razzaq, T. M., Bass, R., Vines, D. J., Werner, F., Whawell, S. A., Ellis, V. (2003). Functional Regulation of Tissue Plasminogen Activator on the Surface of Vascular Smooth Muscle Cells by the Type-II Transmembrane Protein p63 (CKAP4). J. Biol. Chem. 278: 42679-42685 [Abstract] [Full Text]
Klopfenstein, D. R., Klumperman, J., Lustig, A., Kammerer, R. A., Oorschot, V., Hauri, H.-P. (2001). Subdomain-Specific Localization of Climp-63 (P63) in the Endoplasmic Reticulum Is Mediated by Its Luminal {alpha}-Helical Segment. JCB 153: 1287-1300 [Abstract] [Full Text]
Lee, S., Yoon, J., Park, B., Jun, Y., Jin, M., Sung, H. C., Kim, I.-H., Kang, S., Choi, E.-J., Ahn, B. Y., Ahn, K. (2000). Structural and Functional Dissection of Human Cytomegalovirus US3 in Binding Major Histocompatibility Complex Class I Molecules. J. Virol. 74: 11262-11269 [Abstract] [Full Text]
Chen, C., Ma, J., Lazic, A., Backovic, M., Colley, K. J. (2000). Formation of Insoluble Oligomers Correlates with ST6Gal I Stable Localization in the Golgi. J. Biol. Chem. 275: 13819-13826 [Abstract] [Full Text]
Beuret, N., Rutishauser, J., Bider, M. D., Spiess, M. (1999). Mechanism of Endoplasmic Reticulum Retention of Mutant Vasopressin Precursor Caused by a Signal Peptide Truncation Associated with Diabetes Insipidus. J. Biol. Chem. 274: 18965-18972 [Abstract] [Full Text]
Prince, L. S., Welsh, M. J. (1999). Effect of subunit composition and Liddle's syndrome mutations on biosynthesis of ENaC. Am. J. Physiol. Cell Physiol. 276: C1346-C1351 [Abstract] [Full Text]
Jaskiewicz, E., Zhu, G., Bassi, R., Darling, D. S., Young, W. W. Jr. (1996). beta 1,4-N-Acetylgalactosaminyltransferase (GM2 Synthase) Is Released from Golgi Membranes as a Neuraminidase-sensitive, Disulfide-bonded Dimer by a Cathepsin D-like Protease. J. Biol. Chem. 271: 26395-26403 [Abstract] [Full Text]
Hay, J. C., Hirling, H., Scheller, R. H. (1996). Mammalian Vesicle Trafficking Proteins of the Endoplasmic Reticulum and Golgi Apparatus. J. Biol. Chem. 271: 5671-5679 [Abstract] [Full Text]
Szczesna-Skorupa, E., Ahn, K., Chen, C.-D., Doray, B., Kemper, B. (1995). The Cytoplasmic and N-terminal Transmembrane Domains of Cytochrome P450 Contain Independent Signals for Retention in the Endoplasmic Reticulum. J. Biol. Chem. 270: 24327-24333 [Abstract] [Full Text]
Schweizer, A., Rohrer, J., Kornfeld, S. (1995). Determination of the Structural Requirements for Palmitoylation of p63. J. Biol. Chem. 270: 9638-9644 [Abstract] [Full Text]
Locker, J. K., Opstelten, D.-J. E., Ericsson, M., Horzinek, M. C., Rottier, P. J. M. (1995). Oligomerization of a trans-Golgi/ trans-Golgi Network Retained Protein Occurs in the Golgi Complex and May Be Part of Its Retention. J. Biol. Chem. 270: 8815-8821 [Abstract] [Full Text]
Schweizer, A, Rohrer, J, Slot, J., Geuze, H., Kornfeld, S (1995). Reassessment of the subcellular localization of p63. J. Cell Sci. 108: 2477-2485 [Abstract]
Szczesna-Skorupa, E., Kemper, B. (2000). Endoplasmic Reticulum Retention Determinants in the Transmembrane and Linker Domains of Cytochrome P450 2C1. J. Biol. Chem. 275: 19409-19415 [Abstract] [Full Text]