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Related Concept Videos

Golgi Matrix Proteins01:12

Golgi Matrix Proteins

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Golgi matrix proteins are a group of highly dynamic proteins that maintain the stacked structure of Golgi. These proteins adapt to rapid morphological changes of the Golgi during the cell cycle. During cell division, mild proteolysis removes these connections resulting in Golgi unstacking. In The daughter cells, these proteins help reassemble the unstacked Golgi.
One of the first identified Golgi matrix proteins was GM130, a rod-like protein located in the cis-Golgi. Subsequently, many Golgi...
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Transport Across the Golgi01:26

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While it is unclear how molecules move between adjacent Golgi cisternae, it is apparent that the molecules move from cis- cisterna, the entry face, to the trans- cisterna, the exit face. Experiments initially suggested vesicles that bud from one cisterna and fuse with the next cisterna to transport proteins between the cisternae. This vesicular transport model describes the Golgi apparatus as a relatively static structure with a unique enzyme composition in each cisterna. Molecules are...
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Translocation of Proteins into the Mitochondria01:19

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Mitochondrial precursors are translocated to the internal subcompartments via independent mechanisms involving distinct protein machineries called translocases.
Sorting of outer membrane proteins:
Mitochondrial outer membrane proteins are of two types: the transmembrane, beta-barrel porins, and the membrane-anchored, alpha-helical proteins. Beta-barrel porin precursors are translocated by the TOM complex and inserted into the outer mitochondrial membrane by the SAM complex. In contrast,...
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Tail-anchoring of Proteins in the ER Membrane01:45

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Tail-anchored, or TA, proteins are estimated to make up to 3-5% of membrane proteins found in the eukaryotic cell. Such proteins have a single transmembrane domain located approximately 30 amino acid residues upstream from the C-terminal end. As a result, the signal recognition particle (SRP) cannot guide a TA protein to the ER membrane for cotranslational insertion. Hence, they are integrated into the ER membrane post-translationally using their C-terminal end as the anchor. TA proteins...
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Golgi Apparatus01:49

Golgi Apparatus

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As they leave the Endoplasmic Reticulum (ER), properly folded and assembled proteins are selectively packaged into vesicles. These vesicles are transported by microtubule-based motor proteins and fuse together to form vesicular tubular clusters, subsequently arriving at the Golgi apparatus, a eukaryotic endomembrane organelle that often has a distinctive ribbon-like appearance.
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Golgi Apparatus01:09

Golgi Apparatus

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Properly folded and assembled proteins are selectively packaged into vesicles that exit the ER. Motor proteins transport these vesicles to the Golgi apparatus for adding modifications that make these proteins functional at their destination.
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Related Experiment Video

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Quantitative Localization of a Golgi Protein by Imaging Its Center of Fluorescence Mass
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Multiple features within the syntaxin Sed5p mediate its Golgi localization.

Guanbin Gao1, David K Banfield1

  • 1The Division of Life Science, The Hong Kong University of Science and Technology, Hong Kong.

Traffic (Copenhagen, Denmark)
|December 29, 2019
PubMed
Summary
This summary is machine-generated.

Golgi protein Sed5p localization relies on its conformation and COPI binding. This understanding is key to Golgi biogenesis and homeostasis in yeast cells.

Keywords:
COPI-coatomerSNAREsSly1pUfe1pprotein sortingyeast

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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • Golgi apparatus biogenesis and homeostasis depend on protein and lipid transport.
  • Soluble N-ethylmaleimide-sensitive factor attachment protein receptors (SNAREs) are crucial membrane proteins mediating fusion events within the Golgi.
  • Sed5p, a syntaxin SNARE, regulates membrane fusion in the Golgi of budding yeast.

Purpose of the Study:

  • To determine the mechanisms governing Sed5p localization and trafficking within the Golgi.
  • To elucidate the role of Sed5p's structural domains in its Golgi residence.

Main Methods:

  • Conformational analysis of Sed5p.
  • Investigating the role of the Habc domain and SNARE-motif in Sed5p localization.
  • Assessing the impact of the tribasic COPI-coatomer binding motif on intra-Golgi retention.

Main Results:

  • Sed5p's steady-state Golgi localization is primarily conformation-dependent, involving intra-molecular associations between the Habc domain and SNARE-motif.
  • The tribasic COPI-coatomer binding motif is implicated in Sed5p's intra-Golgi retention.

Conclusions:

  • Sed5p localization is regulated by its intrinsic conformation and interactions with coatomer complexes.
  • Understanding Sed5p regulation provides insights into Golgi sorting and homeostasis mechanisms.