Insights into the Function of the Unstructured N-Terminal Domain of Proteins 4.1R and 4.1G in Erythropoiesis
Membrane skeletal protein 4.1R is the prototypical member of a family of four highly paralogous proteins that include 4.1G, 4.1N, and 4.1B. Two isoforms of 4.1R (4.1R135 and 4.1R80), as well as 4.1G, are expressed in erythroblasts during terminal differentiation, but only 4.1R80 is present in mature...
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| Format: | Article |
| Language: | English |
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Wiley
2011-01-01
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| Series: | International Journal of Cell Biology |
| Online Access: | http://dx.doi.org/10.1155/2011/943272 |
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| author | Wataru Nunomura Philippe Gascard Yuichi Takakuwa |
| author_facet | Wataru Nunomura Philippe Gascard Yuichi Takakuwa |
| author_sort | Wataru Nunomura |
| collection | DOAJ |
| description | Membrane skeletal protein 4.1R is the prototypical member of a family of four highly paralogous proteins that include 4.1G, 4.1N, and 4.1B. Two isoforms of 4.1R (4.1R135 and 4.1R80), as well as 4.1G, are expressed in erythroblasts during terminal differentiation, but only 4.1R80 is present in mature erythrocytes. One goal in the field is to better understand the complex regulation of cell type and isoform-specific expression of 4.1 proteins. To start answering these questions, we are studying in depth the important functions of 4.1 proteins in the organization and function of the membrane skeleton in erythrocytes. We have previously reported that the binding profiles of 4.1R80 and 4.1R135 to membrane proteins and calmodulin are very different despite the similar structure of the membrane-binding domain of 4.1G and 4.1R135. We have accumulated evidence for those differences being caused by the N-terminal 209 amino acids headpiece region (HP). Interestingly, the HP region is an unstructured domain. Here we present an overview of the differences and similarities between 4.1 isoforms and paralogs. We also discuss the biological significance of unstructured domains. |
| format | Article |
| id | doaj-art-af1d7aaf17df4db3a7eb5f46906811b4 |
| institution | OA Journals |
| issn | 1687-8876 1687-8884 |
| language | English |
| publishDate | 2011-01-01 |
| publisher | Wiley |
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| series | International Journal of Cell Biology |
| spelling | doaj-art-af1d7aaf17df4db3a7eb5f46906811b42025-08-20T02:19:16ZengWileyInternational Journal of Cell Biology1687-88761687-88842011-01-01201110.1155/2011/943272943272Insights into the Function of the Unstructured N-Terminal Domain of Proteins 4.1R and 4.1G in ErythropoiesisWataru Nunomura0Philippe Gascard1Yuichi Takakuwa2Department of Biochemistry, Tokyo Women's Medical University, Kawada 8-1, Shinjuku, Tokyo 162-8666, JapanDepartment of Pathology, University of California, San Francisco (UCSF), San Francisco, CA 94143-0511, USADepartment of Biochemistry, Tokyo Women's Medical University, Kawada 8-1, Shinjuku, Tokyo 162-8666, JapanMembrane skeletal protein 4.1R is the prototypical member of a family of four highly paralogous proteins that include 4.1G, 4.1N, and 4.1B. Two isoforms of 4.1R (4.1R135 and 4.1R80), as well as 4.1G, are expressed in erythroblasts during terminal differentiation, but only 4.1R80 is present in mature erythrocytes. One goal in the field is to better understand the complex regulation of cell type and isoform-specific expression of 4.1 proteins. To start answering these questions, we are studying in depth the important functions of 4.1 proteins in the organization and function of the membrane skeleton in erythrocytes. We have previously reported that the binding profiles of 4.1R80 and 4.1R135 to membrane proteins and calmodulin are very different despite the similar structure of the membrane-binding domain of 4.1G and 4.1R135. We have accumulated evidence for those differences being caused by the N-terminal 209 amino acids headpiece region (HP). Interestingly, the HP region is an unstructured domain. Here we present an overview of the differences and similarities between 4.1 isoforms and paralogs. We also discuss the biological significance of unstructured domains.http://dx.doi.org/10.1155/2011/943272 |
| spellingShingle | Wataru Nunomura Philippe Gascard Yuichi Takakuwa Insights into the Function of the Unstructured N-Terminal Domain of Proteins 4.1R and 4.1G in Erythropoiesis International Journal of Cell Biology |
| title | Insights into the Function of the Unstructured N-Terminal Domain of Proteins 4.1R and 4.1G in Erythropoiesis |
| title_full | Insights into the Function of the Unstructured N-Terminal Domain of Proteins 4.1R and 4.1G in Erythropoiesis |
| title_fullStr | Insights into the Function of the Unstructured N-Terminal Domain of Proteins 4.1R and 4.1G in Erythropoiesis |
| title_full_unstemmed | Insights into the Function of the Unstructured N-Terminal Domain of Proteins 4.1R and 4.1G in Erythropoiesis |
| title_short | Insights into the Function of the Unstructured N-Terminal Domain of Proteins 4.1R and 4.1G in Erythropoiesis |
| title_sort | insights into the function of the unstructured n terminal domain of proteins 4 1r and 4 1g in erythropoiesis |
| url | http://dx.doi.org/10.1155/2011/943272 |
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