scholarly journals Coupling of Transmembrane Helix Orientation To Membrane Release of the Juxtamembrane Region in FGFR3

Biochemistry ◽  
2014 ◽  
Vol 53 (30) ◽  
pp. 5000-5007 ◽  
Author(s):  
Hiroko Tamagaki ◽  
Yusuke Furukawa ◽  
Ritsuko Yamaguchi ◽  
Hironobu Hojo ◽  
Saburo Aimoto ◽  
...  
Keyword(s):  
Transmembrane Helix ◽  
Juxtamembrane Region ◽  
Helix Orientation

scholarly journals Transmembrane helix orientation influences membrane binding of the intracellular juxtamembrane domain in Neu receptor peptides

2013 ◽  
Vol 110 (5) ◽  
pp. 1646-1651 ◽  
Author(s):  
C. Matsushita ◽  
H. Tamagaki ◽  
Y. Miyazawa ◽  
S. Aimoto ◽  
S. O. Smith ◽  
...  
Keyword(s):  
Transmembrane Helix ◽  
Membrane Binding ◽  
Juxtamembrane Domain ◽  
Helix Orientation

scholarly journals The Polybasic Juxtamembrane Region of Sso1p Is Required for SNARE Function In Vivo

2005 ◽  
Vol 4 (12) ◽  
pp. 2017-2028 ◽  
Author(s):  
Jeffrey S. Van Komen ◽  
Xiaoyang Bai ◽  
Travis L. Rodkey ◽  
Johanna Schaub ◽  
James A. McNew
Keyword(s):  
Plasma Membrane ◽  
Membrane Fusion ◽  
Transmembrane Domain ◽  
Transmembrane Helix ◽  
Specific Interaction ◽  
Coiled Coil ◽  
Snare Complex ◽  
Juxtamembrane Region

ABSTRACT Exocytosis in Saccharomyces cerevisiae requires the specific interaction between the plasma membrane t-SNARE complex (Sso1/2p;Sec9p)and a vesicular v-SNARE (Snc1/2p). While SNARE proteins drive membrane fusion, many aspects of SNARE assembly and regulation are ill defined. Plasma membrane syntaxin homologs (including Sso1p) contain a highly charged juxtamembrane region between the transmembrane helix and the“ SNARE domain” or core complex domain. We examined this region in vitro and in vivo by targeted sequence modification, including insertions and replacements. These modified Sso1 proteins were expressed as the sole copy of Sso in S. cerevisiae and examined for viability. We found that mutant Sso1 proteins with insertions or duplications show limited function, whereas replacement of as few as three amino acids preceding the transmembrane domain resulted in a nonfunctional SNARE in vivo. Viability is also maintained when two proline residues are inserted in the juxtamembrane of Sso1p, suggesting that helical continuity between the transmembrane domain and the core coiled-coil domain is not absolutely required. Analysis of these mutations in vitro utilizing a reconstituted fusion assay illustrates that the mutant Sso1 proteins are only moderately impaired in fusion. These results suggest that the sequence of the juxtamembrane region of Sso1p is vital for function in vivo, independent of the ability of these proteins to direct membrane fusion.

scholarly journals Influence of Paired Histidine Residues on Transmembrane Helix Orientation and Dynamics

2017 ◽  
Vol 112 (3) ◽  
pp. 528a
Author(s):  
Fahmida Afrose ◽  
Denise V. Greathouse ◽  
Roger E. Koeppe
Keyword(s):  
Transmembrane Helix ◽  
Histidine Residues ◽  
Helix Orientation
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