Skip to main content
PMC home page
Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1995 Jan 17;92(2):527–531. doi: 10.1073/pnas.92.2.527

Transcytosis-associated protein (TAP)/p115 is a general fusion factor required for binding of vesicles to acceptor membranes.

M Barroso 1, D S Nelson 1, E Sztul 1
PMCID: PMC42774  PMID: 7831324

Abstract

Transcytosis-associated protein (TAP) is found on transytotic vesicles (TCVs) and is required for their fusion with the target membrane. We developed a cell-free assay capable of differentiating targeting/binding of TCVs to membrane from later fusion events. We found that TAP mediates stable association of TCVs with the target membrane. The sequence of rat liver TAP (959-amino acid open reading frame) encodes a protein that contains (i) an N-terminal region (amino acids 1-649), (ii) an internal region with several coiled-coil stretches (amino acids 650-930), and (iii) a C-terminal acidic region (amino acids 931-959). Comparisons between TAP and other sequences indicate that TAP is identical to p115, a protein involved in cis to medial Golgi transport, and homologous to Uso1p, a yeast protein involved in endoplasmic reticulum to Golgi transport. Our findings suggest that TAP/p115/Usop1 is a general factor acting within the secretory and endocytic pathways to bind transport vesicles prior to membrane fusion.

Full text

PDF
527

Images in this article

528Fig. 1
on p.528
528Fig. 2
on p.528
529Fig. 4
on p.529

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Apodaca G., Katz L. A., Mostov K. E. Receptor-mediated transcytosis of IgA in MDCK cells is via apical recycling endosomes. J Cell Biol. 1994 Apr;125(1):67–86. doi: 10.1083/jcb.125.1.67. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Barroso M., Sztul E. S. Basolateral to apical transcytosis in polarized cells is indirect and involves BFA and trimeric G protein sensitive passage through the apical endosome. J Cell Biol. 1994 Jan;124(1-2):83–100. doi: 10.1083/jcb.124.1.83. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Clary D. O., Griff I. C., Rothman J. E. SNAPs, a family of NSF attachment proteins involved in intracellular membrane fusion in animals and yeast. Cell. 1990 May 18;61(4):709–721. doi: 10.1016/0092-8674(90)90482-t. [DOI] [PubMed] [Google Scholar]
  4. Elazar Z., Orci L., Ostermann J., Amherdt M., Tanigawa G., Rothman J. E. ADP-ribosylation factor and coatomer couple fusion to vesicle budding. J Cell Biol. 1994 Feb;124(4):415–424. doi: 10.1083/jcb.124.4.415. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Espreafico E. M., Cheney R. E., Matteoli M., Nascimento A. A., De Camilli P. V., Larson R. E., Mooseker M. S. Primary structure and cellular localization of chicken brain myosin-V (p190), an unconventional myosin with calmodulin light chains. J Cell Biol. 1992 Dec;119(6):1541–1557. doi: 10.1083/jcb.119.6.1541. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Ferro-Novick S., Jahn R. Vesicle fusion from yeast to man. Nature. 1994 Jul 21;370(6486):191–193. doi: 10.1038/370191a0. [DOI] [PubMed] [Google Scholar]
  7. Kozak M. The scanning model for translation: an update. J Cell Biol. 1989 Feb;108(2):229–241. doi: 10.1083/jcb.108.2.229. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Musil L. S., Baenziger J. U. Proteolytic processing of rat liver membrane secretory component. Cleavage activity is localized to bile canalicular membranes. J Biol Chem. 1988 Oct 25;263(30):15799–15808. [PubMed] [Google Scholar]
  9. Nakajima H., Hirata A., Ogawa Y., Yonehara T., Yoda K., Yamasaki M. A cytoskeleton-related gene, uso1, is required for intracellular protein transport in Saccharomyces cerevisiae. J Cell Biol. 1991 Apr;113(2):245–260. doi: 10.1083/jcb.113.2.245. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Pierre P., Scheel J., Rickard J. E., Kreis T. E. CLIP-170 links endocytic vesicles to microtubules. Cell. 1992 Sep 18;70(6):887–900. doi: 10.1016/0092-8674(92)90240-d. [DOI] [PubMed] [Google Scholar]
  11. Rothman J. E., Warren G. Implications of the SNARE hypothesis for intracellular membrane topology and dynamics. Curr Biol. 1994 Mar 1;4(3):220–233. doi: 10.1016/s0960-9822(00)00051-8. [DOI] [PubMed] [Google Scholar]
  12. Sapperstein S. K., Walter D. M., Grosvenor A. R., Heuser J. E., Waters M. G. p115 is a general vesicular transport factor related to the yeast endoplasmic reticulum to Golgi transport factor Uso1p. Proc Natl Acad Sci U S A. 1995 Jan 17;92(2):522–526. doi: 10.1073/pnas.92.2.522. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Sztul E. S., Howell K. E., Palade G. E. Intracellular and transcellular transport of secretory component and albumin in rat hepatocytes. J Cell Biol. 1983 Nov;97(5 Pt 1):1582–1591. doi: 10.1083/jcb.97.5.1582. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Sztul E., Colombo M., Stahl P., Samanta R. Control of protein traffic between distinct plasma membrane domains. Requirement for a novel 108,000 protein in the fusion of transcytotic vesicles with the apical plasma membrane. J Biol Chem. 1993 Jan 25;268(3):1876–1885. [PubMed] [Google Scholar]
  15. Sztul E., Kaplin A., Saucan L., Palade G. Protein traffic between distinct plasma membrane domains: isolation and characterization of vesicular carriers involved in transcytosis. Cell. 1991 Jan 11;64(1):81–89. doi: 10.1016/0092-8674(91)90210-p. [DOI] [PubMed] [Google Scholar]
  16. Söllner T., Whiteheart S. W., Brunner M., Erdjument-Bromage H., Geromanos S., Tempst P., Rothman J. E. SNAP receptors implicated in vesicle targeting and fusion. Nature. 1993 Mar 25;362(6418):318–324. doi: 10.1038/362318a0. [DOI] [PubMed] [Google Scholar]
  17. Südhof T. C., De Camilli P., Niemann H., Jahn R. Membrane fusion machinery: insights from synaptic proteins. Cell. 1993 Oct 8;75(1):1–4. [PubMed] [Google Scholar]
  18. Warrick H. M., De Lozanne A., Leinwand L. A., Spudich J. A. Conserved protein domains in a myosin heavy chain gene from Dictyostelium discoideum. Proc Natl Acad Sci U S A. 1986 Dec;83(24):9433–9437. doi: 10.1073/pnas.83.24.9433. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Waters M. G., Clary D. O., Rothman J. E. A novel 115-kD peripheral membrane protein is required for intercisternal transport in the Golgi stack. J Cell Biol. 1992 Sep;118(5):1015–1026. doi: 10.1083/jcb.118.5.1015. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Wattenberg B. W., Balch W. E., Rothman J. E. A novel prefusion complex formed during protein transport between Golgi cisternae in a cell-free system. J Biol Chem. 1986 Feb 15;261(5):2202–2207. [PubMed] [Google Scholar]
  21. Whiteheart S. W., Rossnagel K., Buhrow S. A., Brunner M., Jaenicke R., Rothman J. E. N-ethylmaleimide-sensitive fusion protein: a trimeric ATPase whose hydrolysis of ATP is required for membrane fusion. J Cell Biol. 1994 Aug;126(4):945–954. doi: 10.1083/jcb.126.4.945. [DOI] [PMC free article] [PubMed] [Google Scholar]

Articles from Proceedings of the National Academy of Sciences of the United States of America are provided here courtesy of National Academy of Sciences

RESOURCES