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| - | <StructureSection load='3daw' size='340' side='right' caption='Structure of twinfilin-1 C-terminal ADF-H domain (green) complex with actin (grey), ATP and Ca+2 ion (green (PDB code [[3daw]])' scene=''> | + | <StructureSection load='3daw' size='400' side='right' caption='Structure of twinfilin-1 C-terminal ADF-H domain (green) complex with actin (cyan), ATP and Ca+2 ion (green (PDB code [[3daw]])' scene='80/805029/Cv/1'> |
| - | | + | __TOC__ |
| | == Function == | | == Function == |
| | | | |
| | '''Twinfilin''' (Twi) is an actin-monomer-binding protein which is composed of 2 Actin Depolimerizing Factor Homology (ADF-H) domains. Twi forms a 1:1 complex with ADP-actin-monomer, inhibits nucleotide exchange on actin monomers and prevents assembly of the monomer to filaments<ref>PMID:11870207</ref>. | | '''Twinfilin''' (Twi) is an actin-monomer-binding protein which is composed of 2 Actin Depolimerizing Factor Homology (ADF-H) domains. Twi forms a 1:1 complex with ADP-actin-monomer, inhibits nucleotide exchange on actin monomers and prevents assembly of the monomer to filaments<ref>PMID:11870207</ref>. |
| | + | *'''Twinfilin 1''' is an actin-depolymerisation factor regulating actin filament assembly <ref>PMID:35168059</ref>. |
| | + | *'''Twinfilin 2''' regulates stereocilia elongation for maintaining the architecture of cochlear hair bundles<ref>PMID:19955359</ref>. |
| | | | |
| | == Relevance == | | == Relevance == |
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| | == Structural highlights == | | == Structural highlights == |
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| - | The twinfilin-1 C-terminal ADF-H domain binds to a groove between two subdomains of actin. Three major sites of interaction can be distinguished. These interactions include hydrogen bonds and hydrophobic contacts<ref>PMID:18625842</ref>. | + | The twinfilin-1 C-terminal ADF-H domain binds to a groove between two subdomains of actin. <scene name='80/805029/Cv/6'>Three major sites of interaction can be distinguished</scene>. These interactions include <scene name='80/805029/Cv/7'>hydrogen bonds</scene> (twinfilin residues participating in interactions are colored in magenta) and <scene name='80/805029/Cv/8'>hydrophobic contacts</scene> (actin residues participating in interactions are colored according to hydrophobic/polar)<ref>PMID:18625842</ref>. |
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| - | </StructureSection>
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| | | | |
| | ==3D structures of twinfilin== | | ==3D structures of twinfilin== |
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| | + | [[2vac]] – hTwi-2 N-terminal ADF-H domain - human<br /> |
| | + | [[2w0i]] – hTwi-2 C-terminal ADF-H domain (mutant) <br /> |
| | + | [[7ccc]] – hTwi-1 + F-actin-capping protein + actin<br /> |
| | [[2hd7]], [[2d8b]] – mTwi-1 C-terminal ADF-H domain – mouse - NMR<br /> | | [[2hd7]], [[2d8b]] – mTwi-1 C-terminal ADF-H domain – mouse - NMR<br /> |
| | [[1m4j]] – mTwi-1 N-terminal ADF-H domain <br /> | | [[1m4j]] – mTwi-1 N-terminal ADF-H domain <br /> |
| - | [[3daw]] – Twi-1 C-terminal ADF-H domain (mutant) + actin + ATP - rabbit<br /> | + | [[6rsw]] – mTwi-1 C-terminal ADF-H domain + actin + CAP1<br /> |
| - | [[2vac]] – hTwi-2 N-terminal ADF-H domain - human<br /> | + | [[7ds2]] – mTwi-1 C-terminal + F-actin-capping protein<br /> |
| - | [[2w0i]] – hTwi-2 C-terminal ADF-H domain (mutant) <br /> | + | [[7ds4]] – mTwi-1 C-terminal (mutant) + F-actin-capping protein<br /> |
| - | | + | [[7dsb]] – mTwi-1 C-terminal + F-actin-capping protein + myotrophin<br /> |
| | + | [[7ds3]] – mTwi-2 + F-actin-capping protein<br /> |
| | + | [[6yp9]] – rTwi-1 C-terminal ADF-H domain + actin - rabbit<br /> |
| | + | [[3daw]] – rTwi-1 C-terminal ADF-H domain (mutant) + actin + ATP<br /> |
| | + | [[6k2f]] – Twi – ''Entamoeba histolytica''<br /> |
| | | | |
| | == References == | | == References == |
| | <references/> | | <references/> |
| - | | + | </StructureSection> |
| | [[Category:Topic Page]] | | [[Category:Topic Page]] |
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Function
Twinfilin (Twi) is an actin-monomer-binding protein which is composed of 2 Actin Depolimerizing Factor Homology (ADF-H) domains. Twi forms a 1:1 complex with ADP-actin-monomer, inhibits nucleotide exchange on actin monomers and prevents assembly of the monomer to filaments[1].
- Twinfilin 1 is an actin-depolymerisation factor regulating actin filament assembly [2].
- Twinfilin 2 regulates stereocilia elongation for maintaining the architecture of cochlear hair bundles[3].
Relevance
Twi-1 is highly induced by stimulation of amino acids (Met and Leu) and hormones(estrogen and prolactin) and involved in regulation of milk biosynthesis[4].
Structural highlights
The twinfilin-1 C-terminal ADF-H domain binds to a groove between two subdomains of actin. . These interactions include (twinfilin residues participating in interactions are colored in magenta) and (actin residues participating in interactions are colored according to hydrophobic/polar)[5].
3D structures of twinfilin
Updated on 20-August-2024
Domains: N-terminal ADF-H 1-142; C-terminal ADF-H 176-316
2vac – hTwi-2 N-terminal ADF-H domain - human
2w0i – hTwi-2 C-terminal ADF-H domain (mutant)
7ccc – hTwi-1 + F-actin-capping protein + actin
2hd7, 2d8b – mTwi-1 C-terminal ADF-H domain – mouse - NMR
1m4j – mTwi-1 N-terminal ADF-H domain
6rsw – mTwi-1 C-terminal ADF-H domain + actin + CAP1
7ds2 – mTwi-1 C-terminal + F-actin-capping protein
7ds4 – mTwi-1 C-terminal (mutant) + F-actin-capping protein
7dsb – mTwi-1 C-terminal + F-actin-capping protein + myotrophin
7ds3 – mTwi-2 + F-actin-capping protein
6yp9 – rTwi-1 C-terminal ADF-H domain + actin - rabbit
3daw – rTwi-1 C-terminal ADF-H domain (mutant) + actin + ATP
6k2f – Twi – Entamoeba histolytica
References
- ↑ Palmgren S, Vartiainen M, Lappalainen P. Twinfilin, a molecular mailman for actin monomers. J Cell Sci. 2002 Mar 1;115(Pt 5):881-6. PMID:11870207
- ↑ Nguyen MT, Won YH, Kwon TW, Lee W. Twinfilin-1 is an essential regulator of myogenic differentiation through the modulation of YAP in C2C12 myoblasts. Biochem Biophys Res Commun. 2022 Apr 9;599:17-23. PMID:35168059 doi:10.1016/j.bbrc.2022.02.021
- ↑ Peng AW, Belyantseva IA, Hsu PD, Friedman TB, Heller S. Twinfilin 2 regulates actin filament lengths in cochlear stereocilia. J Neurosci. 2009 Dec 2;29(48):15083-8. PMID:19955359 doi:10.1523/JNEUROSCI.2782-09.2009
- ↑ Li L, Liu L, Qu B, Li X, Gao X, Zhang M. Twinfilin 1 enhances milk bio-synthesis and proliferation of bovine mammary epithelial cells via the mTOR signaling pathway. Biochem Biophys Res Commun. 2017 Oct 21;492(3):289-294. doi:, 10.1016/j.bbrc.2017.08.130. Epub 2017 Aug 31. PMID:28864421 doi:http://dx.doi.org/10.1016/j.bbrc.2017.08.130
- ↑ Paavilainen VO, Oksanen E, Goldman A, Lappalainen P. Structure of the actin-depolymerizing factor homology domain in complex with actin. J Cell Biol. 2008 Jul 14;182(1):51-9. PMID:18625842 doi:10.1083/jcb.200803100
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