Protein Modification by RNA‐Dependent Posttranslational Aminoacylation in Synaptoplasm

Gower, David J.; Tytell, Michael

doi:10.1111/j.1471-4159.1986.tb04514.x

Cited by 10 publications

(1 citation statement)

References 37 publications

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“…Movements of SR components may also contribute to the physiological status of pineal SRs. Another possibility is that SR-associated proteins undergo post-translational modification (Gower and Tytell 1986 ; Wu and Lynch 2006 ), which accounts for the day/night changes of pineal melatonin synthesis in certain species (Schomerus and Korf 2005 ).…”

Section: Discussionmentioning

confidence: 99%

Active zone proteins are dynamically associated with synaptic ribbons in rat pinealocytes

et al. 2008

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Synaptic ribbons (SRs) are prominent organelles that are abundant in the ribbon synapses of sensory neurons where they represent a specialization of the cytomatrix at the active zone (CAZ). SRs occur not only in neurons, but also in neuroendocrine pinealocytes where their function is still obscure. In this study, we report that pinealocyte SRs are associated with CAZ proteins such as Bassoon, Piccolo, CtBP1, Munc13-1, and the motorprotein KIF3A and, therefore, consist of a protein complex that resembles the ribbon complex of retinal and other sensory ribbon synapses. The pinealocyte ribbon complex is biochemically dynamic. Its protein composition changes in favor of Bassoon, Piccolo, and Munc13-1 at night and in favor of KIF3A during the day, whereas CtBP1 is equally present during the night and day. The diurnal dynamics of the ribbon complex persist under constant darkness and decrease after stimulus deprivation of the pineal gland by constant light. Our findings indicate that neuroendocrine pinealocytes possess a protein complex that resembles the CAZ of ribbon synapses in sensory organs and whose dynamics are under circadian regulation.

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Section: Discussionmentioning

confidence: 99%

Active zone proteins are dynamically associated with synaptic ribbons in rat pinealocytes

et al. 2008

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N-Terminal arginylation of proteins in explants of injured sciatic nerves and embryonic brains of rats

Chakraborty

Hassankhani

et al. 1993

Neurochem Res

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Posttranslational modification of proteins by arginine and lysine has been demonstrated in crude extracts of vertebrate nerves and brain but not in intact cells. In the present experiments we have exploited the fact that Arg is added posttranslationally only at the N-terminus of target proteins, to demonstrate these reactions in intact cells of sciatic nerves and embryonic brains of rats. Sciatic nerves were crushed in anaesthesized rats and 2 hrs later segments of nerve, including the site of the crush, were removed and incubated in media containing [3H]Arg. Incorporation of [3H]Arg into total proteins was analyzed by acid precipitation and the presence of label at the N-terminus was determined by a modification of the Edman degradation procedure. Approximately 25% of protein bound [3H]Arg was released from the N-terminus by the Edman reaction indicating that it was added posttranslationally rather than through protein synthesis. N-terminal labeling was not detectable in nerves not crushed prior to explant and incubation. Slices of embryonic day 20 visual cortex, when incubated under similar conditions as injured sciatic nerves, also showed approximately 25% of the protein incorporated [3H]Arg at the N-terminus, while arginylation was not detectable in adult rat brain slices. Since Lys is not added posttranslationally to the N-terminus, we have attempted to observe lysylation of proteins in intact cells by using cycloheximide (Cx) to block protein synthesis without interfering with protein modification. The posttranslational incorporation of Arg/Lys into proteins was found to be insensitive to up to 2.0 mM Cx in tissue extracts (in vitro).(ABSTRACT TRUNCATED AT 250 WORDS)

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Regulation of the post-translational conjugation of amino acids to rat brain proteins

1990

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Protein Modification by RNA‐Dependent Posttranslational Aminoacylation in Synaptoplasm

Cited by 10 publications

References 37 publications

Active zone proteins are dynamically associated with synaptic ribbons in rat pinealocytes

Active zone proteins are dynamically associated with synaptic ribbons in rat pinealocytes

N-Terminal arginylation of proteins in explants of injured sciatic nerves and embryonic brains of rats

Regulation of the post-translational conjugation of amino acids to rat brain proteins

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