Cell. Mol. Life Sci. (2013) 70:4199–4200 DOI 10.1007/s00018-013-1473-3
Cellular and Molecular Life Sciences
ERRATUM
Erratum to: Strategies for identifying synthetic peptides to act as inhibitors of NADPH oxidases, or ‘‘All that you did and did not want to know about Nox inhibitory peptides’’ Iris Dahan · Edgar Pick
Published online: 13 September 2013 © Springer Basel 2013
Erratum to: Cell. Mol. Life Sci. (2012) 69:2283–2305 DOI 10.1007/s00018‑012‑1007‑4 The original publication of this article unfortunately contained an error in figure. In page number 2286, Fig. 3: 1. The activation domain in p67phox (residues 199–210), was mislabelled as D. This is now corrected to AD; 2. The numbering of residues in the SH3-N region of p67phox was erroneously shown as starting at 243 and ending at 289. The correct numbering should start with 243 and end with 298. The correct figure is given below.
The online version of the original article can be found under doi:10.1007/s00018-012-1007-4. I. Dahan · E. Pick (*) The Julius Friedrich Cohnheim Laboratory of Phagocyte Research, Department of Clinical Microbiology and Immunology, Sackler School of Medicine, Tel Aviv University, Tel Aviv, Israel e-mail:
[email protected]
13
4200
I. Dahan, E. Pick 4
121
p47phox 1
3
p67phox 1
36
1
1
40
Switch I
TPR 4
60
AD
67
PRR
Switch II
284 292 340
SH3-C
298
351
PX
429
135 159 162
460
228 SH3
515 526
SH3-C
183 188 189
p67phox BD 2
173
390
PRR
PB1
Insert
136
363 368
polybasic
SH3-N
124
Fig. 3 ‘‘The mechanics - those who make the engine work’’. Mapping the protein–protein interaction domains in the cytosolic NADPH oxidase components. The presentation of the domains was inspired by [4]. PX phox homology domain, SH3-N N-terminal src 3 homology domain, SH3-C C-terminal src 3 homology domain, PRR proline-rich
13
229
199- 226210 236 243
70 104 120 153
18
p40phox
214
SH3-N
TPR 1 TPR 2 TPR 3
30
Rac1
159
PX
polybasic
237
192 CLLL
192
329 PB1
339
region, TPR tetratricopeptide repeat, AD activation domain, PB1 Phox and Bem domain, Insert insert region characteristic of Rho proteins, p67phox BD2 second Rac-binding domain on p67phox (in addition to switch I), CLLL C-terminal residues in Rac1 involved in isoprenylation, carboxymethylation, and cleavage of the three leucines