Literature DB >> 21040294

Unraveling the Golgi ribbon.

Jen-Hsuan Wei1, Joachim Seemann.   

Abstract

The Golgi apparatus lies at the heart of the secretory pathway where it receives, modifies and sorts protein cargo to the proper intracellular or extracellular location. Although this secretory function is highly conserved throughout the eukaryotic kingdom, the structure of the Golgi complex is arranged very differently among species. In particular, Golgi membranes in vertebrate cells are integrated into a single compact entity termed the Golgi ribbon that is normally localized in the perinuclear area and in close vicinity to the centrosomes. This organization poses a challenge for cell division when the single Golgi ribbon needs to be partitioned into the two daughter cells. To ensure faithful inheritance in the progeny, the Golgi ribbon is divided in three consecutive steps in mitosis, namely disassembly, partitioning and reassembly. However, the structure of the Golgi ribbon is only present in higher animals and Golgi disassembly during mitosis is not ubiquitous in all organisms. Therefore, there must be unique reasons to build up the Golgi in this particular conformation and to preserve it over generations. In this review, we first highlight the diversity of the Golgi architecture in different organisms and revisit the concept of the Golgi ribbon. Following on, we discuss why the ribbon is needed and how it forms in vertebrate cells. Lastly, we conclude with likely purposes of mitotic ribbon disassembly and further propose mechanisms by which it regulates mitosis.
© 2010 John Wiley & Sons A/S.

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Year:  2010        PMID: 21040294      PMCID: PMC4221251          DOI: 10.1111/j.1600-0854.2010.01114.x

Source DB:  PubMed          Journal:  Traffic        ISSN: 1398-9219            Impact factor:   6.215


  129 in total

1.  mRNA localization and ER-based protein sorting mechanisms dictate the use of transitional endoplasmic reticulum-golgi units involved in gurken transport in Drosophila oocytes.

Authors:  Bram Herpers; Catherine Rabouille
Journal:  Mol Biol Cell       Date:  2004-09-22       Impact factor: 4.138

2.  Mapping the functional domains of the Golgi stacking factor GRASP65.

Authors:  Yanzhuang Wang; Ayano Satoh; Graham Warren
Journal:  J Biol Chem       Date:  2004-12-02       Impact factor: 5.157

3.  The role of GRASP55 in Golgi fragmentation and entry of cells into mitosis.

Authors:  Juan Manuel Duran; Matt Kinseth; Carine Bossard; David W Rose; Roman Polishchuk; Christine C Wu; John Yates; Timo Zimmerman; Vivek Malhotra
Journal:  Mol Biol Cell       Date:  2008-04-02       Impact factor: 4.138

Review 4.  Evolution and diversity of the Golgi body.

Authors:  Kevin Mowbrey; Joel B Dacks
Journal:  FEBS Lett       Date:  2009-10-20       Impact factor: 4.124

5.  Induction of asymmetrical cell division to analyze spindle-dependent organelle partitioning using correlative microscopy techniques.

Authors:  Jen-Hsuan Wei; Joachim Seemann
Journal:  Nat Protoc       Date:  2009-10-22       Impact factor: 13.491

6.  GRASP65, a protein involved in the stacking of Golgi cisternae.

Authors:  F A Barr; M Puype; J Vandekerckhove; G Warren
Journal:  Cell       Date:  1997-10-17       Impact factor: 41.582

7.  Rab11 regulates recycling through the pericentriolar recycling endosome.

Authors:  O Ullrich; S Reinsch; S Urbé; M Zerial; R G Parton
Journal:  J Cell Biol       Date:  1996-11       Impact factor: 10.539

8.  Novel genetic tools reveal Cdk5's major role in Golgi fragmentation in Alzheimer's disease.

Authors:  Kai-Hui Sun; Yolanda de Pablo; Fabien Vincent; Emmanuel O Johnson; Angela K Chavers; Kavita Shah
Journal:  Mol Biol Cell       Date:  2008-05-14       Impact factor: 4.138

9.  The mitotic spindle mediates inheritance of the Golgi ribbon structure.

Authors:  Jen-Hsuan Wei; Joachim Seemann
Journal:  J Cell Biol       Date:  2009-02-02       Impact factor: 10.539

10.  Golgi cisternal unstacking stimulates COPI vesicle budding and protein transport.

Authors:  Yanzhuang Wang; Jen-Hsuan Wei; Blaine Bisel; Danming Tang; Joachim Seemann
Journal:  PLoS One       Date:  2008-02-20       Impact factor: 3.240

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  41 in total

Review 1.  Modular organization of the mammalian Golgi apparatus.

Authors:  Nobuhiro Nakamura; Jen-Hsuan Wei; Joachim Seemann
Journal:  Curr Opin Cell Biol       Date:  2012-06-20       Impact factor: 8.382

Review 2.  Golgi tubules: their structure, formation and role in intra-Golgi transport.

Authors:  Emma Martínez-Alonso; Mónica Tomás; José A Martínez-Menárguez
Journal:  Histochem Cell Biol       Date:  2013-06-29       Impact factor: 4.304

3.  Somatic PI3K activity regulates transition to the spermatocyte stages in Drosophila testis.

Authors:  Samir Gupta; Krishanu Ray
Journal:  J Biosci       Date:  2017-06       Impact factor: 1.826

4.  Growth of the Mammalian Golgi Apparatus during Interphase.

Authors:  Alex T-W Sin; Rene E Harrison
Journal:  Mol Cell Biol       Date:  2016-08-26       Impact factor: 4.272

5.  Stochastic Model of Maturation and Vesicular Exchange in Cellular Organelles.

Authors:  Quentin Vagne; Pierre Sens
Journal:  Biophys J       Date:  2018-02-27       Impact factor: 4.033

6.  Mitotic Golgi disassembly is required for bipolar spindle formation and mitotic progression.

Authors:  Gianni Guizzunti; Joachim Seemann
Journal:  Proc Natl Acad Sci U S A       Date:  2016-10-10       Impact factor: 11.205

7.  Wiskott-Aldrich syndrome protein senses irradiation-induced DNA damage to coordinate the cell-protective Golgi dispersal response in human T and B lymphocytes.

Authors:  Kuo-Kuang Wen; Seong-Su Han; Yatin M Vyas
Journal:  J Allergy Clin Immunol       Date:  2019-10-09       Impact factor: 10.793

Review 8.  How Rab proteins determine Golgi structure.

Authors:  Shijie Liu; Brian Storrie
Journal:  Int Rev Cell Mol Biol       Date:  2015-02-07       Impact factor: 6.813

Review 9.  Cell cycle regulation of Golgi membrane dynamics.

Authors:  Danming Tang; Yanzhuang Wang
Journal:  Trends Cell Biol       Date:  2013-02-28       Impact factor: 20.808

10.  Golgi fragmentation is Rab and SNARE dependent in cellular models of Parkinson's disease.

Authors:  Wilson O Rendón; Emma Martínez-Alonso; Mónica Tomás; Narcisa Martínez-Martínez; José A Martínez-Menárguez
Journal:  Histochem Cell Biol       Date:  2012-12-02       Impact factor: 4.304

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