Ultraviolet light-responsive element (TGACAACA,) -binding proteins in cells of xeroderma pigmentosum patients

1995 ◽  
Vol 14 (2) ◽  
pp. 111-117 ◽  
Author(s):  
Yang Ming Yang ◽  
Zeev Ronai
2015 ◽  
Vol 24 (4) ◽  
pp. 296-297 ◽  
Author(s):  
Christiane Kuschal ◽  
Sikandar G. Khan ◽  
Benedikt Enk ◽  
John J. DiGiovanna ◽  
Kenneth H. Kraemer

1973 ◽  
Vol 13 (3) ◽  
pp. 799-809
Author(s):  
A. MICHAELS ◽  
A. GIBOR

The structural changes associated with the ultraviolet-induced bleaching of light-grown cells of Euglena gracilis were investigated. Our light- and electron-microscopic observations of the bleaching process indicate that there is a continuity of plastid structure in cells 5 generations after receiving a bleaching dose of ultraviolet light. There seems to be a continuous dilution of the plastid thylakoids and a decrease in plastid size in the bleaching cells. There also seems to be a change in the position of the plastids in relation to the mitochondria in the bleaching cells. The plastids and possibly the mitochondria are the only organelles which are affected by the ultraviolet irradiation. The continuity of plastids in bleaching cells of Euglena is discussed in relation to the proposed effect of the ultraviolet light.


1971 ◽  
Vol 44 (2) ◽  
pp. 433-438 ◽  
Author(s):  
Werner E.G. Müller ◽  
Zen-Ichi Yamazaki ◽  
Rudolf K. Zahn ◽  
Georg Brehm ◽  
Günter Korting

2012 ◽  
Vol 23 (4) ◽  
pp. 701-715 ◽  
Author(s):  
David E. Hokanson ◽  
Anthony P. Bretscher

Cell function requires the integration of cytoskeletal organization and membrane trafficking. Small GTP-binding proteins are key regulators of these processes. We find that EPI64, an apical microvillar protein with a Tre-2/Bub2/Cdc16 (TBC) domain that stabilizes active Arf6 and has RabGAP activity, regulates Arf6-dependent membrane trafficking. Expression of EPI64 in HeLa cells induces the accumulation of actin-coated vacuoles, a distinctive phenotype seen in cells expressing constitutively active Arf6. Expression of EPI64 with defective RabGAP activity does not induce vacuole formation. Coexpression of Rab8a suppresses the vacuole phenotype induced by EPI64, and EPI64 expression lowers the level of Rab8-GTP in cells, strongly suggesting that EPI64 has GAP activity toward Rab8a. JFC1, an effector for Rab8a, colocalizes with and binds directly to a C-terminal region of EPI64. Together this region and the N-terminal TBC domain of EPI64 are required for the accumulation of vacuoles. Through analysis of mutants that uncouple JFC1 from either EPI64 or from Rab8-GTP, our data suggest a model in which EPI64 binds JFC1 to recruit Rab8a-GTP for deactivation by the RabGAP activity of EPI64. We propose that EPI64 regulates membrane trafficking both by stabilizing Arf6-GTP and by inhibiting the recycling of membrane through the tubular endosome by decreasing Rab8a-GTP levels.


1998 ◽  
Vol 253 (2) ◽  
pp. 430-436 ◽  
Author(s):  
Florian Guthmann ◽  
Carsten Hohoff ◽  
Henry Fechner ◽  
Peter Humbert ◽  
Torsten Borchers ◽  
...  

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