Genetic and Developmental Characterization of Dmca1D, a Calcium Channel α1 Subunit Gene in Drosophila melanogaster

Genetics ◽  
1998 ◽  
Vol 148 (3) ◽  
pp. 1159-1169
Author(s):  
Daniel F Eberl ◽  
Dejian Ren ◽  
Guoping Feng ◽  
Lori J Lorenz ◽  
David Van Vactor ◽  
...  

Abstract To begin unraveling the functional significance of calcium channel diversity, we identified mutations in Dmca1D, a Drosophila calcium channel α1 subunit cDNA that we recently cloned. These mutations constitute the l(2)35Fa lethal locus, which we rename Dmca1D. A severe allele, Dmca1DX10, truncates the channel after the IV-S4 transmembrane domain. These mutants die as late embryos because they lack vigorous hatching movements. In the weaker allele, Dmca1DAR66, a cysteine in transmembrane domain I-S1 is changed to tyrosine. Dmca1DAR66 embryos hatch but pharate adults have difficulty eclosing. Those that do eclose have difficulty in fluid-filling of the wings. These studies show that this member of the calcium channel α1 subunit gene family plays a nonredundant, vital role in larvae and adults.

1999 ◽  
Vol 14 (3) ◽  
pp. 386-395 ◽  
Author(s):  
Juan C. Loza ◽  
Lillian C. Carpio ◽  
Peter G. Bradford ◽  
Rosemary Dziak

10.1038/947 ◽  
1998 ◽  
Vol 19 (3) ◽  
pp. 264-267 ◽  
Author(s):  
N. Torben Bech-Hansen ◽  
Margaret J. Naylor ◽  
Tracy A. Maybaum ◽  
William G. Pearce ◽  
Ben Koop ◽  
...  

2000 ◽  
Vol 45 (23) ◽  
pp. 2172-2176
Author(s):  
Jiahui Xia ◽  
Huali Zhang ◽  
Dongsheng Tang ◽  
Xixiang Tang ◽  
Heping Dai ◽  
...  

2008 ◽  
Vol 62 (4) ◽  
pp. 1643-1646 ◽  
Author(s):  
Inwha Kang ◽  
David G. Lindquist ◽  
T. Bernard Kinane ◽  
Louis Ercolani ◽  
Gary A. Pritchard ◽  
...  

Gene ◽  
2006 ◽  
Vol 366 (1) ◽  
pp. 117-127 ◽  
Author(s):  
Esther Wong ◽  
Wei-Ping Yu ◽  
Wai Ho Yap ◽  
Byrappa Venkatesh ◽  
Tuck Wah Soong

2004 ◽  
Vol 32 (3) ◽  
pp. 412-415 ◽  
Author(s):  
R. Li ◽  
J.S. Bennett ◽  
W.F. DeGrado

We have expressed two proteins that correspond to the transmembrane and cytoplasmic domains of integrin αIIb and β3 subunits. Characterization of these proteins, dispersed in anionic and zwitterionic micelles, revealed that, rather than interacting with each other, the two proteins associated into homodimers and homotrimers respectively. Moreover, studies using the TOXCAT assay system confirmed that the αIIb and β3 transmembrane domains can self-associate in biological cell membranes. Transmembrane domain-mediated homo-oligomerization provides a plausible structural basis for integrin clustering and could promote integrin activation as well. Indeed, replacing specific residues in the transmembrane helix of either αIIb or β3 with an asparagine residue resulted in a facilitated homo-oligomerization of the mutated transmembrane helix, promoted the formation of integrin clusters on the cell surface and shifted αIIbβ3 to its activated state. Thus these studies support the hypothesis that the transmembrane domains play a vital role in the function and regulation of αIIbβ3.


1997 ◽  
Vol 230 (1) ◽  
pp. 147-154 ◽  
Author(s):  
Tadashi Kimura ◽  
Osamu Shouno ◽  
Kiyonori Hirota ◽  
Takehiko Saito ◽  
Gen Matsumoto ◽  
...  

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