Evidence map›Paper›PMID 41718973›Full record

ReviewSub-cellular biochemistry2026

The Functions of the Golgin Family of Coiled-Coil Proteins.

Maraym Arab, Martin Lowe

Abstract readReview
PubMed Publisher
In one paragraph

Review in Sub-cellular biochemistry, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

0 citing papers in PubMed.

No citing paper in PubMed yet.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

2 authors.

Maraym ArabSchool of Biological Sciences, Faculty of Biology, Medicine and Health, University of Manchester, Manchester, UK.
Martin LoweSchool of Biological Sciences, Faculty of Biology, Medicine and Health, University of Manchester, Manchester, UK. martin.p.lowe@manchester.ac.uk.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The golgins are a family of ubiquitously expressed and evolutionary conserved Golgi-localised coiled-coil proteins. The golgins are particularly important for vesicle trafficking and structural organisation of the Golgi apparatus. The golgins mediate tethering, or long-range capture, of transport vesicles to Golgi membranes, a key step in vesicle traffic that ensures the specificity of vesicle transport at the Golgi. Following tethering, the golgins associate with other factors to ensure that vesicles undergo the transition to membrane fusion mediated by SNARE proteins. The golgins also contribute to the structural organisation of the Golgi apparatus, particularly in Golgi ribbon formation. This is achieved in several ways, which includes linking the Golgi membranes to the microtubule cytoskeleton, controlling the activity of cytoskeletal regulators and physically linking Golgi elements into the ribbon. Golgin-dependent interactions with the microtubule cytoskeleton also contribute to cell polarity, migration and division. In addition to regulating Golgi function and organisation, the golgins scaffold various factors to control the activity of these factors in a range of cellular processes which includes signaling, autophagy, spindle assembly and cell fate determination. In this book chapter we discuss current understanding of the golgins and their functional roles in cells.

Indexed as

Golgi ApparatusMembrane ProteinsAnimalsGolgi Matrix ProteinsHumansMicrotubulesGolgi Matrix ProteinsMembrane ProteinsGolginGolgi ribbonGolgi structureMembrane trafficRab GTPaseVesicle tethering

Identifiers

What OpenQuestion holds

Textmetadata
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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.