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Both types of ribosomes are responsible for protein synthesis.

The rough ER has ribosomes attached to it, and is the site for protein synthesis.

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d. ribosomessite of protein synthesis

As we all have a fair idea regarding production of proteins, the deoxyribonucleic acid (DNA) first produces RNA (messenger RNA or mRNA) by the process of DNA transcription, after which genetic message from the mRNA is translated into proteins during DNA translation.

To be more precise about protein synthesis by ribosomes, the sequence for assembling amino acids during protein synthesis are specified in the mRNA.

Smooth ER is devoid of ribosomes, and is the site for lipid synthesis and protein transport.

One of the first proteins described affecting coelomocyte endocytic function was CUP-5, a homologue of human mucolipin-1, mutations in which leads to mucolipidosis type IV, a lysosomal storage disease in humans (). CUP-5/mucolipin family proteins are thought to act as Ca2+ channels, allowing regulated efflux of Ca2+ from lysosomes. Lysosomal function is strongly impaired in mutants, with very poor cargo degradation in many cell types. mutants display severe defects in lysosome biogenesis that result in the formation of grossly enlarged vacuoles bearing mixed markers for late endosomes and lysosomes (). In wild-type animals CUP-5 labels the lysosome limiting membrane ().

They are responsible for protein synthesis

Overall, the nucleus is responsible for protein synthesis, cell growth, division, and development.

This whole process of protein synthesis is also referred to as central dogma.

Usually, the proteins synthesized by the free ribosomes are utilized in the cytoplasm itself, while the protein molecules produced by the bound ribosomes are transported outside the cell.

In the biosynthetic pathway transmembrane proteins and secretory proteins are synthesized in the ER. Many such proteins are then sorted into COPII coated vesicles at distinct ER-exit sites that transport cargo to the Golgi (). Most of these proteins are then delivered from the -Golgi network (TGN) to destinations such as the plasma membrane, endosomes, and lysosomes. Many proteins that function within the ER are actively recycled from the Golgi to the ER via COPI-mediated retrograde transport, a process required to maintain their ER localization. Similarly, many proteins require COPI-mediated retrograde transport from - to -Golgi compartments to maintain their usual position within the Golgi stack. Transport from the TGN to endosomes or lysosomes is mediated by clathrin-coated vesicles associated with adaptor protein complexes AP1 and GGA1. Most transport from the Golgi to the plasma membrane is thought to be clathrin-independent, although some secretory cargo in epithelial cells is now thought to reach the plasma membrane in an AP1/clathrin-dependent manner ().

Which organelle is responsible for protein synthesis

Roughendoplasmic reticulum, the organelle responsible for protein synthesis, isabundant in the cell body.

It's supported by a meshy network called the nuclear lamina.

To separate the nucleus, genetic material and nuclear activity from outside intrusions, like ions, solutes, and macromolecules.

To manufacture ribosomes.

Made up of ribosomal subunits.

Stores genes in the form of chromosomes, which allows for cell division
Transports gene products by way of nuclear pores
Produces the messages that code for proteins
Organizes the uncoiling of DNA to replicate important genes.

The cell nucleus consists of the nuclear membrane which is a double membrane that has four layers and large pores through which materials pass.


The rough endoplasmic reticulum is a network of tubules and flattened sacs which are studded with ribosomes.

It is responsible for protein synthesis.

The manufacture of steroid hormones in endocrine cells
The detoxification of organic compounds within liver cells
The release of glucose in liver cells,
Regulating the concentration of calcium ions.

The smooth endoplasmic reticulum is a network of tubules and flattened sacs which are NOT studded with ribosomes.

Cell secretions; meaning it releases things like hormones and neurotransmitters at the cell surface.

A small bubble which is enclosed by lipid bi layer.

Structures used to enable movement of cells or sometimes to propel substances across outer surface of the cell.

67. Site of protein synthesis.
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  • Organelles Involved in Protein Synthesis;

    The mRNA synthesized in the nucleus is then transported to the cytoplasm for further continuation of protein synthesis.

  • protein synthesis occurs at this organelle

    Protein Synthesis

  • Organelle Responsible For Protein Synthesis ..

    16/01/2018 · What organelle is the site of protein synthesis

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Responsible For Protein Synthesis ..

Figure 6. RME-1 is a membrane bending protein required for recycling endosome function. (A) Shows the basal surface of the intestinal cells in animal expressing GFP::RME-1. Note that the tubulovesicular network of basolateral recycling endosomes is labeled by GFP::RME-1. (B) Shows an immuno-EM image of fixed intestinal tissue using an anti-RME-1 antibody. Endogenous RME-1 is restricted to the junction of the vesicular and tubular regions of the recycling endosomes where it is likely to regulate fission of cargo-containing tubules. (C) Purified RME-1 proteins were reconstituted on synthetic liposomes. In the presence of ATPγS, RME-1 assembles in rings (striations on tubules) and squeezes the liposome membranes into narrow tubules in a manner very similar to that of Dynamin (GTPγS).

Ribosomes are responsible for protein synthesis.

72. A protein to be exported will be synthesized on the rough endoplasmic reticulum. From there it will travel via transport vesicle to the Golgi apparatus for processing. From the Golgi it will travel, again via vesicle, to the plasma membrane for release outside the cell.

the site of protein synthesis" ..

RME-1 was first discovered in the yolk transport screens, with null mutants displaying poor endocytosis of YP170::GFP (). Further investigation revealed that poor yolk uptake was due to poor recycling of the yolk receptor RME-2 in oocytes. It was also noted that all mutants displayed an unselected phenotype, progressive vacuolization of the intestine that included formation of vacuoles large enough to recognize at the level of the dissecting microscope. Subsequent work showed that these enlarged organelles labeled for ARF-6 but not RAB-5, accumulated several basolateral cargo proteins including hTAC and hTfR, and filled with basolaterally applied fluid-phase endocytosis markers but not endocytosed lipophilic dye FM 4-64 (; ). These results indicated that RME-1 regulated a late step in basolateral recycling. RME-1 protein labeled a tubulovesicular network of endosomes just below the basolateral surface that resembled the endocytic recycling compartment (recycling endosomes) in mammalian cells () (; ; ). Analysis in mammalian cells showed that the RME-1 homolog EHD1 localized to the endocytic recycling compartment and was required for recycling endosome to plasma membrane transport (; ). The basolateral recycling defects of mutants, but not of mutants, can be suppressed by loss of the PTB domain protein NUM-1/Numb. Current models indicate that NUM-1 is a negative regulator of recycling, although its mechanism is not known ().

Protein Synthesis - Cell Organelles and their functions

79. Nucleus contains the DNA in eukaryotes and the nucleolus region in the nucleus is the site of ribosome synthesis while the nucleoid region is the site in prokaryotic cells where the DNA is contained in the cytoplasm.

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