Zobrazeno 1 - 10
of 52
pro vyhledávání: '"Graham H. Thomas"'
Publikováno v:
PLoS ONE, Vol 9, Iss 4, p e93680 (2014)
It is increasingly recognized that non-erythroid spectrins have roles remote from the plasma membrane, notably in endomembrane trafficking. The large spectrin isoform, βH, partners with Annexin B9 to modulate endosomal processing of internalized pro
Externí odkaz:
https://doaj.org/article/6b9fedd8f8b94556bcac036a59c3dd29
Autor:
Khurts Shilagardi, Eric Schiffhauer, Douglas N. Robinson, Tianzhi Luo, Dong-Hoon Lee, Shuo Li, Graham H. Thomas, Sungmin Son, Rui Duan, Elizabeth H. Chen, Daniel A. Fletcher, Ji Hoon Kim
Spectrin is a membrane skeletal protein best known for its structural role in maintaining cell shape and protecting cells from mechanical damage1-3. Here, we report that spectrin dynamically accumulates and dissolves at the fusogenic synapse, where a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3d51a6ac22cf98cbe312084b1c9ea2a7
Autor:
Seungkyu Lee, Graham H. Thomas
Publikováno v:
Mechanisms of Development. 128:116-128
Epithelial polarity and morphogenesis require the careful coordination of signaling and cytoskeletal elements. In this paper, we describe multiple genetic interactions between the apical cytoskeletal protein β(H) and Rac1 signaling in Drosophila: ac
Autor:
Elizabeth A. Klipfell, Janice A. Williams, Emmanuelle Médina, Graham H. Thomas, André Le Bivic, Daniela C. Zarnescu
Publikováno v:
The Journal of Cell Biology
The apical transmembrane protein Crumbs is necessary for both cell polarization and the assembly of the zonula adherens (ZA) in Drosophila epithelia. The apical spectrin-based membrane skeleton (SBMS) is a protein network that is essential for epithe
Autor:
David W. Speicher, Megan D. Radyk, Sandra L. Harper, Floyd J. Mattie, Stephanie E Crilly, Mansi R. Khanna, Graham H. Thomas, Katelyn J. Bakerink, Kristen C. Browder
Publikováno v:
The Journal of biological chemistry. 290(2)
The dominant paradigm for spectrin function is that (αβ)2-spectrin tetramers or higher order oligomers form membrane-associated two-dimensional networks in association with F-actin to reinforce the plasma membrane. Tetramerization is an essential e
Autor:
Graham H. Thomas
Publikováno v:
BioEssays. 23:152-160
It has long been speculated that spectrin, the actin crosslinking and molecular scaffold protein, is involved in the development of apicobasal polarity in epithelia. While spectrins can undoubtedly influence the protein content of specific membrane d
Autor:
Daniela C. Zarnescu, Graham H. Thomas
Publikováno v:
The Journal of Cell Biology
Changes in cell shape and position drive morphogenesis in epithelia and depend on the polarized nature of its constituent cells. The spectrin-based membrane skeleton is thought to be a key player in the establishment and/or maintenance of cell shape
Autor:
Amy Londergan, Daniel P. Kiehart, Graham H. Thomas, Carol C. Korte, Mark A. Bales, Daniela C. Zarnescu, Amy E. Juedes
Publikováno v:
Development. 125:2125-2134
The spectrin membrane skeleton is a ubiquitous cytoskeletal structure with several cellular roles, including the maintenance of cell integrity, determination of cell shape and as a contributor to cell polarity. We have isolated mutations in the gene
Autor:
M A Bales, Andrew G. Clark, Spencer V. Muse, Graham H. Thomas, Carol C. Korte, E C Newbern, Daniel P. Kiehart
Publikováno v:
Molecular Biology and Evolution. 14:1285-1295
Many structural, signaling, and adhesion molecules contain tandemly repeated amino acid motifs. The alpha-actinin/spectrin/dystrophin superfamily of F-actin-crosslinking proteins contains an array of triple alpha-helical motifs (spectrin repeats). We
Publikováno v:
PLoS ONE
PLoS ONE, Vol 9, Iss 4, p e93680 (2014)
PLoS ONE, Vol 9, Iss 4, p e93680 (2014)
It is increasingly recognized that non-erythroid spectrins have roles remote from the plasma membrane, notably in endomembrane trafficking. The large spectrin isoform, βH, partners with Annexin B9 to modulate endosomal processing of internalized pro