Journal of Molecular Biology
Regular ArticleSurface Tongue-and-groove Contours on Lens MIP Facilitate Cell-to-cell Adherence☆,☆☆
References (46)
- et al.
Cryo-negative staining
Micron
(1998) - et al.
Lens membranes II. Isolation and characterization of the main intrinsic polypeptide (MIP) of bovine lens fiber membranes
Expt. Eye Res.
(1976) - et al.
MRC image-processing programs
J. Struct. Biol.
(1996) - et al.
Reconstruction of glutamine synthetase using computer averaging
Ultramicroscopy
(1978) - et al.
Major intrinsic polypeptide (MIP26K) from the lens membrane: reconstitution into vesicles and inhibition of channel forming activity by peptide antiserum
Biochem. Biophys. Res. Com.
(1985) - et al.
The major intrinsic protein (MIP) of the bovine lens fiber membrane: characterization and structure based on cDNA cloning
Cell
(1984) - et al.
Purified lens major intrinsic protein (MIP) forms highly ordered tetragonal two-dimensional arrays by reconstitution
J. Mol. Biol.
(1998) - et al.
Ion, water and neutral solute transport in Xenopus oocytes expressing frog lens MIP
Expt. Eye Res.
(1995) - et al.
Water channel properties of major intrinsic protein of lens
J. Biol. Chem.
(1995) - et al.
The height of biomolecules measured with the atomic force microscope depends on electrostatic interactions
Biophys. J.
(1997)
Electrostatically balanced subnanometer imaging of biological specimens by atomic force microscope
Biophys. J.
Structure of the water channel AqpZ from Escherichia coli revealed by electron crystallography
J. Mol. Biol.
Reproducible acquisition of Escherichia coli porin surface topographs by atomic force microscopy
Biophys. J.
Surface topographies at subnanometer-resolution reveal asymmetry and sidedness of aquaporin-1
J. Mol. Biol.
The specialized junctions of the lens
Int. Rev. Cytol.
Immunocytochemical localization of the lens main intrinsic polypeptide (MIP26) in communicating junctions
J. Cell Biol.
Liquefaction of cortical tissue in diabetic and galactosemic rat lenses defined by confocal laser scanning microscopy
Invest. Ophthalmol. Vis. Sci.
Comparison of the water transporting properties of MIP and AQP1
J. Membr. Biol.
Distribution of gap junctions and square array junctions in the mammalian lens
Invest. Ophthalmol. Vis. Sci.
Cryo-electron microscopy of vitrified specimens
Quart. Rev. Biophys.
Electron microscopic observations of reconstituted proteoliposomes with the purified major intrinsic membrane protein of eye lens fibers
J. Cell Biol.
Properties of channels reconstituted from the major intrinsic protein of lens fiber membranes
J. Gen. Physiol.
Phosphorylation modulates the voltage dependence of channels reconstituted from the major intrinsic protein of lens fiber membranes
J. Membr. Biol.
Cited by (130)
Phylogenetic characterization of transporter proteins in the cnidarian-dinoflagellate symbiosis
2018, Molecular Phylogenetics and EvolutionIncreased aquaporin 1 and 5 membrane expression in the lens epithelium of cataract patients
2016, Biochimica et Biophysica Acta - Molecular Basis of DiseaseCitation Excerpt :Because of its low water permeability, it has been proposed that AQP0 might be involved in regulating the resistance of the paracellular pathway, rather than in cell membrane water permeability [5,17]. Therefore, proposed mechanisms for the implication of mutations in AQP0 in cataract include loss of AQP0-facilitated fiber-fiber adherence [14] and impaired fiber cell dehydration [18]. With respect to AQP1, cataracts were not reported in human subjects with AQP1 deficiency [19], and spontaneous cataracts are not seen grossly in AQP1 null mice [20].
Assemblies of pore-forming toxins visualized by atomic force microscopy
2016, Biochimica et Biophysica Acta - BiomembranesHigh-speed atomic force microscopy: Imaging and force spectroscopy
2014, FEBS LettersAquaporins in the eye: Expression, function, and roles in ocular disease
2014, Biochimica et Biophysica Acta - General SubjectsCitation Excerpt :The interaction of AQP0 with ezrin/radixin/moesin actin binding proteins [90], with lens specific cytoskeletal proteins filensin and phakinin [91,92], and with gap junction proteins [58,59] may be important for its structural properties. AQP0 has been implicated in junction formation, tongue-and-groove formation, and cell-to-cell adhesion in a number of studies [73,93–95]. As a long-lived protein, AQP0 accumulates numerous modifications during its lifetime [68,96,97].
- ☆
Abbreviations used: AFM, atomic force microscopy; AQP, aquaporin; FRC, Fourier ring correlation function; MIP, major intrinsic protein; PHR, phase residual; SSNR, spectral signal-to-noise ratio
- ☆☆
Edited by G. V. Heijne
- f1
D. F. and L. H. contributed equally to this work.
- f2
Corresponding author
- f3
E-mail address of the corresponding author: [email protected]