这是阎写的信吗
我还以为循正道去信给编辑部呢，原来是走的“野路子”，只在人家网站下留了个评论就溜走了，这算是写信吗？啊，不对，大阎说过在等回信，希望不是在这样等人家来评论，如果是我来评评吧。黑字是大阎的，红的是俺的。
Runtao Yan ? 2 months ago ? edited
Dear Nature,
I would like to provide evidences to show that the mechanism and the topological model of glucose transporter was not first identified by Dr. Nieng Yan’s team reported in this Nature paper (2014,Nature 510:121). Rather,Yan&Maloney had reported the findings published in Cell (1993, Cell 75:37 ) and PNAS (1995, PNAS 92:5973). The Nature paper did not mention the Yan&Maloney model at all, nor in references.
Yan didn’t make any claim that she and her team first identified the mechanism or the topological model of glucose transporter. They stated very clearly in the paper that “On the basis of our structural analysis and published biochemical data, we propose a working model for GLUT1 (Fig. 5).” The key word is "GLUT1"!
They didn't cite your papers because they didn't need to. They cited references that were not only more relevant but also newer.
In 2012, Dr Maloney (Hopkins team) was alive. The Tsinghua team had to cite our papers if they provided the working model, which should be the same as ours. In such consideration, they may worry that the paper could not be accepted by Nature as it just confirmed our model. Dr Maloney died Dec.12, 2013, and Tsinghua team’s 2014 Nature paper was published on May 18, 2014, which showed the glucose transporter working model.
This is not only a pure assumption, but also a shame because a dead person was used as a shield. Yan et al proposed a model for human GLUT1 not XylE, which they published on in 2012. How could they have proposed a model for GLUT1 in 2012 without even knowing how it looked like back then? The statement is just absurd.
You should know that the critical parts of the paper are the crystallization and resolution of the structure, which generated some very useful insights into the mechanism underlying glucose transport by GLUT1. The model is only a tiny part of it. Besides, it is based on the alternate access model, not the one that you proposed! Give your deceased supervisor a break!
In addition,
1. The two teams studied the same family transporters, belong to MFS family or uniporter-symporter-antiporter family, (Microbiol Mol Bio Rev. 1998, 62:1-34) and two glucose transporters share the same 12 transmembrane helix structure.
But they are two different transporters and are expected to have different structures and mechanism of transportation.
2. Evidence 1: the glucose transporter working model....
3. Evidence 2. The detailed topological model....
4. Yan/Maloney model is the earliest experimentally identified sugar transporter working model....
No, it was not. The earliest model is the alternate access model. You only made some modifications to it based on your data about C265.
5.5. Is it possible that the topological working model could be only identified by using active protein, not by crystal protein?....
It is possible as clearly shown by Yan et al. Besides you are not the only one who did experiments with the active protein. Yan et al also did many mutations and generated a lot of BIOCHEMICAL data that were published in their reference 28.
Summary;
Principally and logically, If they could not figure out the glucose transporter working model based on the structure in the 2012 Nature paper, they should not figure out the model based on the similar structure in the 2014 Nature paper either. If this is the case, It is apparent that they could have copied the Yan/Maloney topological model in the 2014 Nature paper.
Yes, they could. As shown in figure 5 and its legend, the model consists of 4 predicted conformations—"outward-open, ligand-bound and occluded, inward-open, and ligand-free and occluded—required for a complete transport cycle according to the alternating access model. The inward-open conformation of GLUT1 is reported in this study. The ligand-bound, occluded conformation and the ligand-free, occluded one are predicted from two XylE structures in the outward-facing, partly occluded and ligand-bound state (28), and the inwardfacing, occluded state (29), respectively. The outward-open structure remains to be captured. The ICH domain is illustrated as a latch that strengthens the intracellular gate in the outward-facing conformations. The extracellular gate comprises a few residues from TM1, TM4 and TM7 that are illustrated by the red brick in the ‘inward open’ cartoon.
