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A crosslinked and ribosylated actin trimer does not interact productively with myosin
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| Zeitschriftentitel: | Biochemistry and Cell Biology |
|---|---|
| Personen und Körperschaften: | , |
| In: | Biochemistry and Cell Biology, 97, 2019, 2, S. 140-147 |
| Format: | E-Article |
| Sprache: | Englisch |
| veröffentlicht: |
Canadian Science Publishing
|
| Schlagwörter: |
| author_facet |
Sidhu, Navneet Dawson, John F. Sidhu, Navneet Dawson, John F. |
|---|---|
| author |
Sidhu, Navneet Dawson, John F. |
| spellingShingle |
Sidhu, Navneet Dawson, John F. Biochemistry and Cell Biology A crosslinked and ribosylated actin trimer does not interact productively with myosin Cell Biology Molecular Biology Biochemistry |
| author_sort |
sidhu, navneet |
| spelling |
Sidhu, Navneet Dawson, John F. 0829-8211 1208-6002 Canadian Science Publishing Cell Biology Molecular Biology Biochemistry http://dx.doi.org/10.1139/bcb-2018-0082 <jats:p>A purified F-actin-derived actin trimer that interacts with end-binding proteins did not activate or bind the side-binding protein myosin under rigor conditions. Remodeling of the actin trimer by the binding of gelsolin did not rescue myosin binding, nor did the use of different means of inhibiting the polymerization of the trimer. Our results demonstrate that ADP-ribosylation on all actin subunits of an F-actin-derived trimer inhibits myosin binding and that the binding of DNase-I to the pointed end subunits of a crosslinked trimer also remodels the myosin binding site. Taken together, this work highlights the need for a careful balance between modification of actin subunits and maintaining protein–protein interactions to produce a physiologically relevant short F-actin complex.</jats:p> A crosslinked and ribosylated actin trimer does not interact productively with myosin Biochemistry and Cell Biology |
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Biochemistry and Cell Biology |
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| title |
A crosslinked and ribosylated actin trimer does not interact productively with myosin |
| title_unstemmed |
A crosslinked and ribosylated actin trimer does not interact productively with myosin |
| title_full |
A crosslinked and ribosylated actin trimer does not interact productively with myosin |
| title_fullStr |
A crosslinked and ribosylated actin trimer does not interact productively with myosin |
| title_full_unstemmed |
A crosslinked and ribosylated actin trimer does not interact productively with myosin |
| title_short |
A crosslinked and ribosylated actin trimer does not interact productively with myosin |
| title_sort |
a crosslinked and ribosylated actin trimer does not interact productively with myosin |
| topic |
Cell Biology Molecular Biology Biochemistry |
| url |
http://dx.doi.org/10.1139/bcb-2018-0082 |
| publishDate |
2019 |
| physical |
140-147 |
| description |
<jats:p>A purified F-actin-derived actin trimer that interacts with end-binding proteins did not activate or bind the side-binding protein myosin under rigor conditions. Remodeling of the actin trimer by the binding of gelsolin did not rescue myosin binding, nor did the use of different means of inhibiting the polymerization of the trimer. Our results demonstrate that ADP-ribosylation on all actin subunits of an F-actin-derived trimer inhibits myosin binding and that the binding of DNase-I to the pointed end subunits of a crosslinked trimer also remodels the myosin binding site. Taken together, this work highlights the need for a careful balance between modification of actin subunits and maintaining protein–protein interactions to produce a physiologically relevant short F-actin complex.</jats:p> |
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| author | Sidhu, Navneet, Dawson, John F. |
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| description | <jats:p>A purified F-actin-derived actin trimer that interacts with end-binding proteins did not activate or bind the side-binding protein myosin under rigor conditions. Remodeling of the actin trimer by the binding of gelsolin did not rescue myosin binding, nor did the use of different means of inhibiting the polymerization of the trimer. Our results demonstrate that ADP-ribosylation on all actin subunits of an F-actin-derived trimer inhibits myosin binding and that the binding of DNase-I to the pointed end subunits of a crosslinked trimer also remodels the myosin binding site. Taken together, this work highlights the need for a careful balance between modification of actin subunits and maintaining protein–protein interactions to produce a physiologically relevant short F-actin complex.</jats:p> |
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| imprint | Canadian Science Publishing, 2019 |
| imprint_str_mv | Canadian Science Publishing, 2019 |
| institution | DE-14, DE-Ch1, DE-L229, DE-D275, DE-Bn3, DE-Brt1, DE-D161, DE-Gla1, DE-Zi4, DE-15, DE-Rs1, DE-Pl11 |
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| physical | 140-147 |
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| series | Biochemistry and Cell Biology |
| source_id | 49 |
| spelling | Sidhu, Navneet Dawson, John F. 0829-8211 1208-6002 Canadian Science Publishing Cell Biology Molecular Biology Biochemistry http://dx.doi.org/10.1139/bcb-2018-0082 <jats:p>A purified F-actin-derived actin trimer that interacts with end-binding proteins did not activate or bind the side-binding protein myosin under rigor conditions. Remodeling of the actin trimer by the binding of gelsolin did not rescue myosin binding, nor did the use of different means of inhibiting the polymerization of the trimer. Our results demonstrate that ADP-ribosylation on all actin subunits of an F-actin-derived trimer inhibits myosin binding and that the binding of DNase-I to the pointed end subunits of a crosslinked trimer also remodels the myosin binding site. Taken together, this work highlights the need for a careful balance between modification of actin subunits and maintaining protein–protein interactions to produce a physiologically relevant short F-actin complex.</jats:p> A crosslinked and ribosylated actin trimer does not interact productively with myosin Biochemistry and Cell Biology |
| spellingShingle | Sidhu, Navneet, Dawson, John F., Biochemistry and Cell Biology, A crosslinked and ribosylated actin trimer does not interact productively with myosin, Cell Biology, Molecular Biology, Biochemistry |
| title | A crosslinked and ribosylated actin trimer does not interact productively with myosin |
| title_full | A crosslinked and ribosylated actin trimer does not interact productively with myosin |
| title_fullStr | A crosslinked and ribosylated actin trimer does not interact productively with myosin |
| title_full_unstemmed | A crosslinked and ribosylated actin trimer does not interact productively with myosin |
| title_short | A crosslinked and ribosylated actin trimer does not interact productively with myosin |
| title_sort | a crosslinked and ribosylated actin trimer does not interact productively with myosin |
| title_unstemmed | A crosslinked and ribosylated actin trimer does not interact productively with myosin |
| topic | Cell Biology, Molecular Biology, Biochemistry |
| url | http://dx.doi.org/10.1139/bcb-2018-0082 |