The C-terminus of prestin influences nonlinear capacitance and plasma membrane targeting

Zheng, Jing; Du, Guo Guang; Matsuda, Keiji; Orem, Alex; Aguiñaga, Sal; Deák, Levente; Navarrete, Enrique; Madison, Laird D.; Dallos, Peter

doi:10.1242/jcs.02431

Cited by 73 publications

(98 citation statements)

References 51 publications

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“…The specificity of these antibodies has been fully characterized and verified in previous studies, including in prestin knockout mice (Zheng et al, 2001(Zheng et al, , 2005Matsuda et al, 2004). In later experiments, we also used other two commercial anti-prestin Cterminal and N-terminal antibodies (cat#: ss-22694 and ss-22692, respectively, Santa Cruz Biotechnology Inc., CA).…”

Section: Prestin Antibodiesmentioning

confidence: 85%

Prestin is expressed on the whole outer hair cell basolateral surface

Zhu

Zhao

2006

Brain Research

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Prestin has been identified as a motor protein responsible for outer hair cell (OHC) electromotility. Previous experiments revealed that OHC electromotility and its associated nonlinear capacitance resided in the OHC lateral wall and was not detected at the apical cuticular plate and basal region. In this experiment, the distribution of prestin in adult mouse, rat, and guinea pig OHCs was reexamined by use of immunofluorescent staining and confocal microscopy. We found that prestin labeling was located at the whole OHC basolateral wall, including the basal plasma membrane. However, staining at the basal membrane was weak. As compared with the intensity at the lateral wall, the intensities of prestin labeling at the membrane at the nuclear level and basal pole were 80.5% and 61.1%, respectively. Prestin labeling was not found at the cuticular plate and stereocilia. The prestin labeling was also absent in the cytoplasm and nuclei. The OHC lateral wall above the nuclear level is composed of the plasma membrane, cortical lattice, and subsurface cisternae. By costaining with di-8-ANEPPS, prestin labeling was found at the outer layer of the OHC lateral wall, which was further evidenced by use of a hypotonic challenge to separate the plasma membrane from the underlying subsurface cisternae. The data revealed that prestin is expressed at the whole OHC basolateral membrane. Prestin in the basal plasma membrane may provide a reservoir on the OHC surface for prestin-recycling and may also facilitate performing its hypothesized transporter function.

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Section: Prestin Antibodiesmentioning

confidence: 85%

Prestin is expressed on the whole outer hair cell basolateral surface

Zhu

Zhao

2006

Brain Research

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“…4) were cloned into a pEGFP-N2 vector as described previously (16). HEK293T cells were then transfected with the mutated prestin-expressing plasmids, and NLC was measured as described previously (20).…”

Section: Generation Of Prestin Mutants and Evaluation Of Nlc In Hek293tmentioning

confidence: 99%

The V499G/Y501H Mutation Impairs Fast Motor Kinetics of Prestin and Has Significance for Defining Functional Independence of Individual Prestin Subunits

Homma

Duan

Zheng

et al. 2013

Journal of Biological Chemistry

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Background: Prestin converts electrical energy into mechanical work. Results: The V499G/Y501H mutation significantly impairs fast motor kinetics of prestin. Conclusion: Impaired kinetics is attributable to mutation at the Val-499 site that is conserved among SLC26 proteins regardless of their function as motors or transporters. Significance: V499G/Y501H mutated prestin provides clues to the molecular mechanisms underlying somatic electromotility and thus cochlear amplification.

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“…Moreover, a series of short truncations in both cytodomains revealed that, despite normal membrane targeting, these mutations resulted in absent or modified prestin activity both in vitro (Navaratnam et al, 2005;Zheng et al, 2005) and in vivo (Dallos et al, 2008). These functional consequences led the authors to suggest that prestin requires interacting partners to drive OHC motor activity (Navaratnam et al, 2005).…”

Section: Localization Of the Conventional Spectrin Subunits In The Aumentioning

confidence: 99%

“…Previous reports have shown that some particular amino acid residues in the C-terminal region play a key role in prestin cellular distribution and motor activity (Navaratnam et al, 2005;Zheng et al, 2005). We produced two prestin mutants, Del632 and Del709, which have been shown to impair the ability of prestin to confer non-linear capacitance and motility (Zheng et al, 2005). Del632 lacks the STAS motif (sulphate transporter and anti-sigma factor antagonist domain, aa 633-708), a domain identified in all ten SLC26A proteins.…”

mentioning

confidence: 99%

αII-βV spectrin bridges the plasma membrane and cortical lattice in the lateral wall of the auditory outer hair cells

Legendre

Safieddine

Küssel-Andermann

et al. 2008

Journal of Cell Science

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The sensitivity and frequency selectivity of the mammalian cochlea involves a mechanical amplification process called electromotility, which requires prestin-dependent length changes of the outer hair cell (OHC) lateral wall in response to changes in membrane electric potential. The cortical lattice, the highly organized cytoskeleton underlying the OHC lateral plasma membrane, is made up of F-actin and spectrin. Here, we show that αII and two of the five β-spectrin subunits, βII and βV, are present in OHCs. βII spectrin is restricted to the cuticular plate, a dense apical network of actin filaments, whereas βV spectrin is concentrated at the cortical lattice. Moreover, we show that αII-βV spectrin directly interacts with F-actin and band 4.1, two components of the OHC cortical lattice. βV spectrin is progressively recruited into the cortical lattice between postnatal day 2 (P2) and P10 in the mouse, in parallel with prestin membrane insertion, which itself parallels the maturation of cell electromotility. Although βV spectrin does not directly interact with prestin, we found that addition of lysates derived from mature auditory organs, but not from the brain or liver, enables βV spectrin-prestin interaction. Using this assay, βV spectrin, via its PH domain, indirectly interacts with the C-terminal cytodomain of prestin. We conclude that the cortical network involved in the sound-induced electromotility of OHCs contains αII-βV spectrin, and not the conventional αII-βII spectrin.Supplementary material available online at http://jcs.biologists.org/cgi/content/full/121/20/3347/DC1 Key words: βV spectrin, Prestin, Outer hair cell, Cortical lattice, Electromotility Summary αII-βV spectrin bridges the plasma membrane and cortical lattice in the lateral wall of the auditory outer hair cells

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The C-terminus of prestin influences nonlinear capacitance and plasma membrane targeting

Cited by 73 publications

References 51 publications

Prestin is expressed on the whole outer hair cell basolateral surface

Prestin is expressed on the whole outer hair cell basolateral surface

The V499G/Y501H Mutation Impairs Fast Motor Kinetics of Prestin and Has Significance for Defining Functional Independence of Individual Prestin Subunits

αII-βV spectrin bridges the plasma membrane and cortical lattice in the lateral wall of the auditory outer hair cells

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