1szv
From Proteopedia
(New page: 200px<br /><applet load="1szv" size="450" color="white" frame="true" align="right" spinBox="true" caption="1szv" /> '''Structure of the Adaptor Protein p14 reveals...) |
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| - | [[Image:1szv.gif|left|200px]]<br /><applet load="1szv" size=" | + | [[Image:1szv.gif|left|200px]]<br /><applet load="1szv" size="350" color="white" frame="true" align="right" spinBox="true" |
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'''Structure of the Adaptor Protein p14 reveals a Profilin-like Fold with Novel Function'''<br /> | '''Structure of the Adaptor Protein p14 reveals a Profilin-like Fold with Novel Function'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The adaptor protein p14 is associated with the cytoplasmic face of late | + | The adaptor protein p14 is associated with the cytoplasmic face of late endosomes that is involved in cell-surface receptor endocytosis and it also directly interacts with MP1, a scaffolding protein that binds the MAP kinase ERK1 and its upstream kinase activator MEK1. The interaction of p14 with MP1 recruits the latter to late endosomes and the endosomal localization of p14/MP1-MEK1-ERK1 scaffolding complex is required for signaling via ERK MAP kinase in an efficient and specific manner upon receptor stimulation. Here, we report the three-dimensional solution structure of the adaptor protein p14. The structure reveals a profilin-like fold with a central five-stranded beta-sheet sandwiched between alpha-helices. Unlike profilin, however, p14 exhibits weak interaction with selective phosphoinositides but no affinity towards proline-rich sequences. Structural comparison between profilin and p14 reveals the molecular basis for the differences in these functions. We further mapped the MP1 binding sites on p14 by NMR, and discuss the implications of these important findings on the possible function of p14. |
==About this Structure== | ==About this Structure== | ||
| - | 1SZV is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http:// | + | 1SZV is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SZV OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Zeng, L.]] | [[Category: Zeng, L.]] | ||
[[Category: Zhang, Q.]] | [[Category: Zhang, Q.]] | ||
| - | [[Category: Zhou, M | + | [[Category: Zhou, M M.]] |
[[Category: p14]] | [[Category: p14]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:08:07 2008'' |
Revision as of 13:08, 21 February 2008
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Structure of the Adaptor Protein p14 reveals a Profilin-like Fold with Novel Function
Overview
The adaptor protein p14 is associated with the cytoplasmic face of late endosomes that is involved in cell-surface receptor endocytosis and it also directly interacts with MP1, a scaffolding protein that binds the MAP kinase ERK1 and its upstream kinase activator MEK1. The interaction of p14 with MP1 recruits the latter to late endosomes and the endosomal localization of p14/MP1-MEK1-ERK1 scaffolding complex is required for signaling via ERK MAP kinase in an efficient and specific manner upon receptor stimulation. Here, we report the three-dimensional solution structure of the adaptor protein p14. The structure reveals a profilin-like fold with a central five-stranded beta-sheet sandwiched between alpha-helices. Unlike profilin, however, p14 exhibits weak interaction with selective phosphoinositides but no affinity towards proline-rich sequences. Structural comparison between profilin and p14 reveals the molecular basis for the differences in these functions. We further mapped the MP1 binding sites on p14 by NMR, and discuss the implications of these important findings on the possible function of p14.
About this Structure
1SZV is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.
Reference
Structure of the adaptor protein p14 reveals a profilin-like fold with distinct function., Qian C, Zhang Q, Wang X, Zeng L, Farooq A, Zhou MM, J Mol Biol. 2005 Mar 25;347(2):309-21. Epub 2005 Jan 27. PMID:15740743
Page seeded by OCA on Thu Feb 21 15:08:07 2008
Categories: Mus musculus | Single protein | Farooq, A. | Qian, C. | Wang, X. | Zeng, L. | Zhang, Q. | Zhou, M M. | P14
