GTP binds to α-crystallin and causes a significant conformational change

Mendoza, Jose A.; Correa, Matthew Daniel; Zardeneta, Gustavo

doi:10.1016/j.ijbiomac.2012.02.015

Cited by 1 publication

(1 citation statement)

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“…Currently, the lectin chaperones calnexin and calreticulin, which are components of the ER quality control system, associate with TYR during protein folding (Petrescu, ). Second, there is no observation of TYRP1 consuming energy to perform the protective function, in contrast to chaperone‐like molecules requiring ATP or GTP as an energy source to perform their function (Biswas & Das, ; Mendoza, Correa, & Zardeneta, ). Third, according to our data, TYRP1 is monomeric and does not form a large oligomeric homocomplex to provide a protein surface for the binding of misfolded proteins, as suggested previously (Glover & Clark, ; Jovcevski et al, ).…”

Section: Discussionmentioning

confidence: 99%

The TYRP1‐mediated protection of human tyrosinase activity does not involve stable interactions of tyrosinase domains

Dolinska

Wingfield

Young

et al. 2019

Pigment Cell Melanoma Res

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Tyrosinases are melanocyte‐specific enzymes involved in melanin biosynthesis. Mutations in their genes cause oculocutaneous albinism associated with reduced or altered pigmentation of skin, hair, and eyes. Here, the recombinant human intra‐melanosomal domains of tyrosinase, TYRtr (19–469), and tyrosinase‐related protein 1, TYRP1tr (25–472), were studied in vitro to define their functional relationship. Proteins were expressed or coexpressed in whole Trichoplusia ni larvae and purified. Their associations were studied using gel filtration and sedimentation equilibrium methods. Protection of TYRtr was studied by measuring the kinetics of tyrosinase diphenol oxidase activity in the presence (1:1 and 1:20 molar ratios) or the absence of TYRP1tr for 10 hr under conditions mimicking melanosomal and ER pH values. Our data indicate that TYRtr incubation with excess TYRP1tr protects TYR, increasing its stability over time. However, this mechanism does not appear to involve the formation of stable hetero‐oligomeric complexes to maintain the protective function.

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Section: Discussionmentioning

confidence: 99%