scholarly journals Relationships between Subcellular Localization, Hub Proteins and Intrinsic Disorder

2017 ◽  
Vol 57 (2) ◽  
pp. 085-089
Author(s):  
Motonori OTA ◽  
Satoshi FUKUCHI ◽  
Ryotaro KOIKE
Keyword(s):  
Subcellular Localization ◽  
Intrinsic Disorder ◽  
Hub Proteins

scholarly journals Intrinsic Disorder Is a Common Feature of Hub Proteins from Four Eukaryotic Interactomes

2006 ◽  
Vol 2 (8) ◽  
pp. e100 ◽  
Author(s):  
Chad Haynes ◽  
Christopher J Oldfield ◽  
Fei Ji ◽  
Niels Klitgord ◽  
Michael E Cusick ◽  
...  
Keyword(s):  
Intrinsic Disorder ◽  
Hub Proteins

Role of intrinsic disorder in transient interactions of hub proteins

2006 ◽  
Vol 66 (4) ◽  
pp. 761-765 ◽  
Author(s):  
Gajinder Pal Singh ◽  
Mythily Ganapathi ◽  
Debasis Dash
Keyword(s):  
Intrinsic Disorder ◽  
Transient Interactions ◽  
Hub Proteins

Exploring the relationship between hub proteins and drug targets based on GO and intrinsic disorder

2015 ◽  
Vol 56 ◽  
pp. 41-48 ◽  
Author(s):  
Yuanyuan Fu ◽  
Yanzhi Guo ◽  
Yuelong Wang ◽  
Jiesi Luo ◽  
Xuemei Pu ◽  
...  
Keyword(s):  
Drug Targets ◽  
Intrinsic Disorder ◽  
The Relationship ◽  
Hub Proteins

scholarly journals Intrinsic Disorder is a Common Feature of Hub Proteins from Four Eukaryotic Interactomes

2005 ◽  
Vol preprint (2006) ◽  
pp. e100 ◽  
Author(s):  
Chad Haynes ◽  
Christopher J Oldfield ◽  
Fei Ji ◽  
Niels Klitgord ◽  
Michael E Cusick ◽  
...  
Keyword(s):  
Intrinsic Disorder ◽  
Hub Proteins

Investigating the functional link between TMEM165 and SPCA1

2019 ◽  
Vol 476 (21) ◽  
pp. 3281-3293 ◽  
Author(s):  
Elodie Lebredonchel ◽  
Marine Houdou ◽  
Hans-Heinrich Hoffmann ◽  
Kateryna Kondratska ◽  
Marie-Ange Krzewinski ◽  
...  
Keyword(s):  
Subcellular Localization ◽  
Complete Loss ◽  
Protein Family ◽  
Uncharacterized Protein ◽  
Functional Link ◽  
P Type

TMEM165 was highlighted in 2012 as the first member of the Uncharacterized Protein Family 0016 (UPF0016) related to human glycosylation diseases. Defects in TMEM165 are associated with strong Golgi glycosylation abnormalities. Our previous work has shown that TMEM165 rapidly degrades with supraphysiological manganese supplementation. In this paper, we establish a functional link between TMEM165 and SPCA1, the Golgi Ca2+/Mn2+ P-type ATPase pump. A nearly complete loss of TMEM165 was observed in SPCA1-deficient Hap1 cells. We demonstrate that TMEM165 was constitutively degraded in lysosomes in the absence of SPCA1. Complementation studies showed that TMEM165 abundance was directly dependent on SPCA1's function and more specifically its capacity to pump Mn2+ from the cytosol into the Golgi lumen. Among SPCA1 mutants that differentially impair Mn2+ and Ca2+ transport, only the Q747A mutant that favors Mn2+ pumping rescues the abundance and Golgi subcellular localization of TMEM165. Interestingly, the overexpression of SERCA2b also rescues the expression of TMEM165. Finally, this paper highlights that TMEM165 expression is linked to the function of SPCA1.

Subcellular localization of GLUT4 in nonstimulated and insulin-stimulated soleus muscle of rat

Diabetes ◽  
1992 ◽  
Vol 41 (2) ◽  
pp. 215-221 ◽  
Author(s):  
A. Bornemann ◽  
T. Ploug ◽  
H. Schmalbruch
Keyword(s):  
Subcellular Localization ◽  
Soleus Muscle
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