scholarly journals R ‐hydroxynitrile lyase from the cyanogenic millipede, Chamberlinius hualienensis —A new entry to the carrier protein family Lipocalines

FEBS Journal ◽  
2020 ◽  
Author(s):  
Fumihiro Motojima ◽  
Atsushi Izumi ◽  
Aem Nuylert ◽  
Zhenyu Zhai ◽  
Mohammad Dadashipour ◽  
...  
Keyword(s):  
Protein Family ◽  
Carrier Protein ◽  
Hydroxynitrile Lyase ◽  
New Entry

scholarly journals Solute carrier protein family 11 member 1 (Slc11a1) activation efficiently inhibits Leishmania donovani survival in host macrophages

2016 ◽  
Vol 41 (3) ◽  
pp. 671-677 ◽  
Author(s):  
Nisha Singh ◽  
Mallikarjuna Rao Gedda ◽  
Neeraj Tiwari ◽  
Suya P. Singh ◽  
Surabhi Bajpai ◽  
...  
Keyword(s):  
Leishmania Donovani ◽  
Protein Family ◽  
Carrier Protein ◽  
Solute Carrier

scholarly journals Role of YHM1, encoding a mitochondrial carrier protein, in iron distribution of yeast

2004 ◽  
Vol 378 (2) ◽  
pp. 599-607 ◽  
Author(s):  
Emmanuel LESUISSE ◽  
Elise R. LYVER ◽  
Simon A. B. KNIGHT ◽  
Andrew DANCIS
Keyword(s):  
Protein Family ◽  
Carrier Protein ◽  
Ferric Reductase ◽  
Mitochondrial Carrier ◽  
Mitochondrial Dna Damage ◽  
Cellular Iron ◽  
Mitochondrial Transporter ◽  
Large Protein Family ◽  
Mitochondrial Carrier Protein ◽  
Mitochondrial Carrier Proteins

Mitochondrial carrier proteins are a large protein family, consisting of 35 members in Saccharomyces cerevisiae. Members of this protein family have been shown to transport varied substrates from cytoplasm to mitochondria or mitochondria to cytoplasm, although many family members do not have assigned substrates. We speculated whether one or more of these transporters will play a role in iron metabolism. Haploid yeast strains each deleted for a single mitochondrial carrier protein were analysed for alterations in iron homoeostasis. The strain deleted for YHM1 was characterized by increased and misregulated surface ferric reductase and high-affinity ferrous transport activities. Siderophore uptake from different sources was also increased, and these effects were dependent on the AFT1 iron sensor regulator. Mutants of YHM1 converted into rho°, consistent with secondary mitochondrial DNA damage from mitochondrial iron accumulation. In fact, in the Δyhm1 mutant, iron was found to accumulate in mitochondria. The accumulated iron showed decreased availability for haem synthesis, measured in isolated mitochondria using endogenously available metals and added porphyrins. The phenotypes of Δyhm1 mutants indicate a role for this mitochondrial transporter in cellular iron homoeostasis.

scholarly journals Not all mitochondrial carrier proteins support permeability transition pore formation: no involvement of uncoupling protein 1

2009 ◽  
Vol 30 (3) ◽  
pp. 187-192 ◽  
Author(s):  
Paul G. Crichton ◽  
Nadeene Parker ◽  
Antonio J. Vidal-Puig ◽  
Martin D. Brand
Keyword(s):  
Cyclosporin A ◽  
Pore Formation ◽  
Uncoupling Protein ◽  
Permeability Transition Pore ◽  
Permeability Transition ◽  
Protein Family ◽  
Carrier Protein ◽  
Uncoupling Protein 1 ◽  
Mitochondrial Carrier ◽  
Mitochondrial Carrier Protein

The mPTP (mitochondrial permeability transition pore) is a non-specific channel that is formed in the mitochondrial inner membrane in response to several stimuli, including elevated levels of matrix calcium. The pore is proposed to be composed of the ANT (adenine nucleotide translocase), voltage-dependent anion channel and cyclophilin D. Knockout studies, however, have demonstrated that ANT is not essential for permeability transition, which has led to the proposal that other members of the mitochondrial carrier protein family may be able to play a similar function to ANT in pore formation. To investigate this possibility, we have studied the permeability transition properties of BAT (brown adipose tissue) mitochondria in which levels of the mitochondrial carrier protein, UCP1 (uncoupling protein 1), can exceed those of ANT. Using an improved spectroscopic assay, we have quantified mPTP formation in de-energized mitochondria from wild-type and Ucp1KO (Ucp1-knockout) mice and assessed the dependence of pore formation on UCP1. When correctly normalized for differences in mitochondrial morphology, we find that calcium-induced mPTP activity is the same in both types of mitochondria, with similar sensitivity to GDP (~50% inhibited), although the portion sensitive to cyclosporin A is higher in mitochondria lacking UCP1 (~80% inhibited, compared with ~60% in mitochondria containing UCP1). We conclude that UCP1 is not a component of the cyclosporin A-sensitive mPTP in BAT and that playing a role in mPTP formation is not a general characteristic of the mitochondrial carrier protein family but is, more likely, restricted to specific members including ANT.

New entry for angiostatic cancer treatment

Blood ◽  
2008 ◽  
Vol 111 (4) ◽  
pp. 1755-1756
Author(s):  
Arjan W. Griffioen
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Cancer Treatment ◽  
Tumor Angiogenesis ◽  
Small Heat Shock Protein ◽  
Protein Family ◽  
New Entry

A member of the small heat shock protein family is found to regulate the formation of vasculature. A study by Dimberg and colleagues combines novel insights into the mechanisms of tumor angiogenesis with therapeutic opportunities for the treatment of cancer.

scholarly journals The 2.1 Å structure of an elicitin-ergosterol complex: A recent addition to the Sterol Carrier Protein family

1999 ◽  
Vol 8 (6) ◽  
pp. 1191-1199 ◽  
Author(s):  
Guillaume Boissy ◽  
Michael O'Donohue ◽  
Odile Gaudemer ◽  
Valérie Perez ◽  
Jean-Claude Pernollet ◽  
...  
Keyword(s):  
Protein Family ◽  
Carrier Protein ◽  
Sterol Carrier Protein ◽  
Recent Addition
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