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Solution structure of the cytohesin-1 (B2-1) Sec7 domain and its interaction with the GTPase ADP ribosylation factor 1.

Betz SF, Schnuchel A, Wang H, Olejniczak ET, Meadows RP, Lipsky BP, Harris EA, Staunton DE, Fesik SW
Proc Natl Acad Sci U S A 95 7909-14 (1998)
Cited: 23 times
EuropePMC logo PMID: 9653114

Abstract

Cytohesin-1 (B2-1) is a guanine nucleotide exchange factor for human ADP ribosylation factor (Arf) GTPases, which are important for vesicular protein trafficking and coatamer assembly in the cell. Cytohesin-1 also has been reported to promote cellular adhesion via binding to the beta2 integrin cytoplasmic domain. The solution structure of the Sec7 domain of cytohesin-1, which is responsible for both the protein's guanine nucleotide exchange factor function and beta2 integrin binding, was determined by NMR spectroscopy. The structure consists of 10 alpha-helices that form a unique tertiary fold. The binding between the Sec7 domain and a soluble, truncated version of human Arf-1 was investigated by examining 1H-15N and 1H-13C chemical shift changes between the native protein and the Sec7/Arf-1 complex. We show that the binding to Arf-1 occurs through a large surface on the C-terminal subdomain that is composed of both hydrophobic and polar residues. Structure-based mutational analysis of the cytohesin-1 Sec7 domain has been used to identify residues important for binding to Arf and for mediating nucleotide exchange. Investigations into the interaction between the Sec7 domain and the beta2 integrin cytoplasmic domain suggest that the two proteins do not interact in the solution phase.

Articles - 1bc9 mentioned but not cited (1)

  1. Solution structure of the cytohesin-1 (B2-1) Sec7 domain and its interaction with the GTPase ADP ribosylation factor 1. Betz SF, Schnuchel A, Wang H, Olejniczak ET, Meadows RP, Lipsky BP, Harris EA, Staunton DE, Fesik SW. Proc Natl Acad Sci U S A 95 7909-7914 (1998)


Reviews citing this publication (5)

  1. Turning on ARF: the Sec7 family of guanine-nucleotide-exchange factors. Jackson CL, Casanova JE. Trends Cell Biol 10 60-67 (2000)
  2. GEFs: structural basis for their activation of small GTP-binding proteins. Cherfils J, Chardin P. Trends Biochem Sci 24 306-311 (1999)
  3. Membranes as messengers in T cell adhesion signaling. Dustin ML, Bivona TG, Philips MR. Nat Immunol 5 363-372 (2004)
  4. The immunological synapse: integrins take the stage. Sims TN, Dustin ML. Immunol Rev 186 100-117 (2002)
  5. Cytohesin-1 in 2001. Moss J, Vaughan M. Arch Biochem Biophys 397 156-161 (2002)

Articles citing this publication (17)

  1. Structural basis for activation of ARF GTPase: mechanisms of guanine nucleotide exchange and GTP-myristoyl switching. Goldberg J. Cell 95 237-248 (1998)
  2. Rap1 is a potent activation signal for leukocyte function-associated antigen 1 distinct from protein kinase C and phosphatidylinositol-3-OH kinase. Katagiri K, Hattori M, Minato N, Irie Sk, Takatsu K, Kinashi T. Mol Cell Biol 20 1956-1969 (2000)
  3. Phylogenetic analysis of Sec7-domain-containing Arf nucleotide exchangers. Cox R, Mason-Gamer RJ, Jackson CL, Segev N. Mol Biol Cell 15 1487-1505 (2004)
  4. NMR structure and mutagenesis of the N-terminal Dbl homology domain of the nucleotide exchange factor Trio. Liu X, Wang H, Eberstadt M, Schnuchel A, Olejniczak ET, Meadows RP, Schkeryantz JM, Janowick DA, Harlan JE, Harris EA, Staunton DE, Fesik SW. Cell 95 269-277 (1998)
  5. ARF-GEP(100), a guanine nucleotide-exchange protein for ADP-ribosylation factor 6. Someya A, Sata M, Takeda K, Pacheco-Rodriguez G, Ferrans VJ, Moss J, Vaughan M. Proc Natl Acad Sci U S A 98 2413-2418 (2001)
  6. Binding site of brefeldin A at the interface between the small G protein ADP-ribosylation factor 1 (ARF1) and the nucleotide-exchange factor Sec7 domain. Robineau S, Chabre M, Antonny B. Proc Natl Acad Sci U S A 97 9913-9918 (2000)
  7. Genetic interactions in yeast between Ypt GTPases and Arf guanine nucleotide exchangers. Jones S, Jedd G, Kahn RA, Franzusoff A, Bartolini F, Segev N. Genetics 152 1543-1556 (1999)
  8. ARL4D recruits cytohesin-2/ARNO to modulate actin remodeling. Li CC, Chiang TC, Wu TS, Pacheco-Rodriguez G, Moss J, Lee FJ. Mol Biol Cell 18 4420-4437 (2007)
  9. Structural basis for the inhibitory effect of brefeldin A on guanine nucleotide-exchange proteins for ADP-ribosylation factors. Sata M, Moss J, Vaughan M. Proc Natl Acad Sci U S A 96 2752-2757 (1999)
  10. Phosphoinositides determine specificity of the guanine-nucleotide exchange activity of cytohesin-1 for ADP-ribosylation factors derived from a mammalian expression system. Knorr T, Nagel W, Kolanus W. Eur J Biochem 267 3784-3791 (2000)
  11. Rapid determination of antigenic epitopes in human NGAL using NMR. Olejniczak ET, Ruan Q, Ziemann RN, Birkenmeyer LG, Saldana SC, Tetin SY. Biopolymers 93 657-667 (2010)
  12. Systematic structure-function analysis of the small GTPase Arf1 in yeast. Click ES, Stearns T, Botstein D. Mol Biol Cell 13 1652-1664 (2002)
  13. Brefeldin A-inhibited guanine nucleotide-exchange protein 3 (BIG3) is predicted to interact with its partner through an ARM-type α-helical structure. Chen YA, Murakami Y, Ahmad S, Yoshimaru T, Katagiri T, Mizuguchi K. BMC Res Notes 7 435 (2014)
  14. B2-1, a Sec7- and pleckstrin homology domain-containing protein, localizes to the Golgi complex. Lee SY, Mansour M, Pohajdak B. Exp Cell Res 256 515-521 (2000)
  15. Structural Dynamics Control Allosteric Activation of Cytohesin Family Arf GTPase Exchange Factors. Malaby AW, Das S, Chakravarthy S, Irving TC, Bilsel O, Lambright DG. Structure 26 106-117.e6 (2018)
  16. Plakophilin-2 induced EGFR phosphorylation: a focus on the intracellular activators of EGFR. Arimoto KI, Weng S, Zhang DE. Receptors Clin Investig 2 e485 (2014)
  17. Letter No Sec7-homology domain in guanine-nucleotide-exchange factors that act on Ras and Rho. Ponting CP, Bork P, Schultz J, Aravind L. Trends Biochem Sci 24 177-178 (1999)


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