scholarly journals Interactions between Transport Protein Particle (TRAPP) complexes and RabGTPases in Arabidopsis

2019 ◽  
Vol 100 (2) ◽  
pp. 279-297 ◽  
Author(s):  
Monika Kalde ◽  
Liam Elliott ◽  
Raksha Ravikumar ◽  
Katarzyna Rybak ◽  
Melina Altmann ◽  
...  
Keyword(s):  
Transport Protein ◽  
Protein Particle

scholarly journals TRAPPopathies: An emerging set of disorders linked to variations in the genes encoding transport protein particle (TRAPP)‐associated proteins

Traffic ◽  
2018 ◽  
Vol 20 (1) ◽  
pp. 5-26 ◽  
Author(s):  
Michael Sacher ◽  
Nassim Shahrzad ◽  
Hiba Kamel ◽  
Miroslav P. Milev
Keyword(s):  
Transport Protein ◽  
Genes Encoding ◽  
Associated Proteins ◽  
Protein Particle

Biochemical consequences of sedlin mutations that cause spondyloepiphyseal dysplasia tarda

2009 ◽  
Vol 423 (2) ◽  
pp. 233-242 ◽  
Author(s):  
Mei Y. Choi ◽  
Caleb C. Y. Chan ◽  
Danny Chan ◽  
Keith D. K. Luk ◽  
Kathryn S. E. Cheah ◽  
...  
Keyword(s):  
Late Onset ◽  
Transport Protein ◽  
Missense Mutations ◽  
Wild Type ◽  
Spondyloepiphyseal Dysplasia ◽  
Type Protein ◽  
Wild Type Protein ◽  
Protein Particle ◽  
Spondyloepiphyseal Dysplasia Tarda

SEDT (spondyloepiphyseal dysplasia tarda) is a late-onset X-linked recessive skeletal dysplasia caused by mutations in the gene SEDL coding for sedlin. In the present paper, we investigated four missense mutations observed in SEDT and compare biochemical and cellular characteristics relative to the wild-type protein to address the mechanism of disease and to gain insight into the function of the sedlin protein. In situ hybridization and immunohistochemical experiments in mouse growth plates revealed sedlin to be predominantly expressed in proliferating and hypertrophic chondrocytes. Cell culture studies showed that the wild-type protein localized predominantly in the vicinity of the nucleus and the Golgi, with further localization around the cytoplasm, whereas mutation resulted in mislocalization. The D47Y mutant was expressed similarly to the wild-type, but the S73L, F83S and V130D mutants showed particularly low levels of expression that were rescued in the presence of the proteasome inhibitor MG132 (benzyloxycarbonyl-leucylleucylleucinal). Furthermore, whereas the D47Y mutant folded similarly and had similar stability to the wild-type sedlin as shown by CD and fluorescence, the S73L, F83S and V130D mutants all misfolded during expression. Two independent assays showed that the D47Y mutation resulted in an increased affinity for the transport protein particle component Bet3 compared with the wild-type sedlin. Our results suggest that the sedlin mutations S73L, F83S and V130D cause SEDT by sedlin misfolding, whereas the D47Y mutation may influence normal TRAPP (transport protein particle) dynamics.

scholarly journals Mutants in trs120 disrupt traffic from the early endosome to the late Golgi

2005 ◽  
Vol 171 (5) ◽  
pp. 823-833 ◽  
Author(s):  
Huaqing Cai ◽  
Yueyi Zhang ◽  
Marc Pypaert ◽  
Lee Walker ◽  
Susan Ferro-Novick
Keyword(s):  
Coat Protein ◽  
Membrane Traffic ◽  
Transport Protein ◽  
Early Endosome ◽  
Specific Gene ◽  
Membrane Structures ◽  
Vesicle Traffic ◽  
Large Complex ◽  
Protein Particle ◽  
Endosomal Pathway

Transport protein particle (TRAPP), a large complex that mediates membrane traffic, is found in two forms (TRAPPI and -II). Both complexes share seven subunits, whereas three subunits (Trs130p, -120p, and -65p) are specific to TRAPPII. Previous studies have shown that mutations in the TRAPPII-specific gene trs130 block traffic through or from the Golgi. Surprisingly, we report that mutations in trs120 do not block general secretion. Instead, trs120 mutants accumulate aberrant membrane structures that resemble Berkeley bodies and disrupt the traffic of proteins that recycle through the early endosome. Mutants defective in recycling also display a defect in the localization of coat protein I (COPI) subunits, implying that Trs120p may participate in a COPI-dependent trafficking step on the early endosomal pathway. Furthermore, we demonstrate that Trs120p largely colocalizes with the late Golgi marker Sec7p. Our findings imply that Trs120p is required for vesicle traffic from the early endosome to the late Golgi.

scholarly journals Characterization of the self-palmitoylation activity of the transport protein particle component Bet3

2010 ◽  
Vol 67 (15) ◽  
pp. 2653-2664 ◽  
Author(s):  
Daniel Kümmel ◽  
Julia Walter ◽  
Martin Heck ◽  
Udo Heinemann ◽  
Michael Veit
Keyword(s):  
Transport Protein ◽  
The Self ◽  
Protein Particle

Intestinal deletion of fatty acid transport protein 4 in mice increases blood chylomicrons

2020 ◽  
Author(s):  
W Chamulitrat ◽  
J Seeßle ◽  
B Javaheri-Haghighi ◽  
S Döring ◽  
X Zhu ◽  
...  
Keyword(s):  
Fatty Acid ◽  
Transport Protein ◽  
Fatty Acid Transport ◽  
Acid Transport ◽  
Fatty Acid Transport Protein

Genetische Ablation des alpha-Tocopherol-Transport-Protein führt zu einem gestörten Kohlenhydratstoffwechsel in der Maus

2004 ◽  
Vol 29 (02) ◽  
Author(s):  
D Pomplun ◽  
C Bumke-Vogt ◽  
N Landes ◽  
P Pfluger ◽  
M Glaubitz ◽  
...  
Keyword(s):  
Transport Protein ◽  
Alpha Tocopherol

Transthyretin – a forgotten thyroid hormone transport protein

1989 ◽  
Vol 120 (3_Suppl) ◽  
pp. S44-S45
Author(s):  
J. RAMAKER ◽  
P. C. SCRIBA ◽  
W. G. WOOD
Keyword(s):  
Thyroid Hormone ◽  
Transport Protein ◽  
Hormone Transport
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