ArticleInvestigative ophthalmology & visual science2009
AlphaB-crystallin: a Golgi-associated membrane protein in the developing ocular lens.
Article in Investigative ophthalmology & visual science, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 19 citations in OpenAlex.
- Insight into the biochemical and cell biological function of an intrinsically unstructured heat shock protein, Hsp12 of Ustilago maydis.Molecular plant pathology · 2023Article
- The interaction of heat shock proteins with cellular membranes: a historical perspective.Cell stress & chaperones · 2021Review
- The small heat shock proteins, HSPB1 and HSPB5, interact differently with lipid membranes.Cell stress & chaperones · 2019Article
- Evolutionary Origins of Pax6 Control of Crystallin Genes.Genome biology and evolution · 2017Article
- Inhibition of the Expression of the Small Heat Shock Protein αB-Crystallin Inhibits Exosome Secretion in Human Retinal Pigment Epithelial Cells in Culture.The Journal of biological chemistry · 2016Article
- Small Heat Shock Protein αB-Crystallin Controls Shape and Adhesion of Glioma and Myoblast Cells in the Absence of Stress.PloS one · 2016Article
- Expression of the HSF4 DNA binding domain-EGFP hybrid gene recreates early childhood lamellar cataract in transgenic mice.Investigative ophthalmology & visual science · 2014Article
- A gene-specific non-enhancer sequence is critical for expression from the promoter of the small heat shock protein gene αB-crystallin.Human genomics · 2014Article
- αA-crystallin and αB-crystallin reside in separate subcellular compartments in the developing ocular lens.The Journal of biological chemistry · 2012Article
- αB-crystallin/sHSP protects cytochrome c and mitochondrial function against oxidative stress in lens and retinal cells.Biochimica et biophysica acta · 2012Article
- Functional validation of hydrophobic adaptation to physiological temperature in the small heat shock protein αA-crystallin.PloS one · 2012Article
- AlphaB-crystallin is found in detergent-resistant membrane microdomains and is secreted via exosomes from human retinal pigment epithelial cells.The Journal of biological chemistry · 2011Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
purposeAll crystallins have non-crystallin catalytic functions. Because catalytic functions do not require large concentrations of protein, as are seen in the lens, there is a perception of dichotomy in the catalytic/physiological function of crystallins within and outside the lens. The status of alphaB-crystallin, a ubiquitously expressed small heat shock protein (and a crystallin) in the ocular lens, was investigated.
methodsDiscontinuous sucrose density gradients were used for fractionation of Golgi membranes and vesicles. Light microscopy and confocal microscopy were used for immunolocalization in cultured cells and the native lens.
resultsalphaB-crystallin is highly organized, as indicated by its polar presence in the apical Golgi in lens epithelium and in the perinuclear Golgi streaks in differentiating lens fiber cells. Assessment of the distribution of alphaB-crystallin in Golgi-enriched and vesicular fractions (characterized by the presence of Golgi membrane protein GM130 and vesicle coat protein gammaCOP) in the developing lens reveal a gradual transition from Golgi to vesicular fraction, concomitant with the appearance of alphaB-crystallin as a "soluble" protein.
conclusionsThese data demonstrate that alphaB-crystallin, known to be a soluble protein, starts life as a Golgi-associated membrane protein in the fetal and early postnatal lens and that the developmentally controlled physical state of the Golgi determines the status of this protein in the lens. These findings also show the similarity in the localization/physiological function of alphaB-crystallin within and outside the ocular lens and suggest that non-crystallin/catalytic function is an innate component of the expression of a crystallin in the lens.
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