Annexin VI isoforms are differentially expressed in mammalian tissues

Kaetzel, Marcia A.; Pula, Grazia; Campos, Begoña; Uhrín, Pavel; Horseman, Nelson D.; Dedman, John R.

doi:10.1016/0167-4889(94)90097-3

Cited by 35 publications

(20 citation statements)

References 33 publications

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“…This is consistent with the finding that the structural differences between the two isoforms due to the lack of the VAAEIL residues alters their functional behavior and interaction with membranes (45). It is likely that, as also noted by others, Anxa6 isoforms interact with different targets and behave differentially in vesicular and endocytic trafficking pathways (36,37).…”

Section: Discussionmentioning

confidence: 99%

“…Anxa6 Is Isoform-specific and "Necessary" but Not "Sufficient" for Evoking ANP-mediated Protection against HypertrophyIsoform specificity has been questioned as a determinant of Anxa6 involvement in vesicular trafficking (36,37). We found that the shorter isoform (lacking the VAAEIL residues between 525-530) of Anxa6 (Anxa6.2), although unnoticeable in control cells, expressed to a detectable limit upon PE treatment (Fig.…”

Section: Scrambshr and H9c2mentioning

confidence: 99%

See 1 more Smart Citation

Cytosolic Dynamics of Annexin A6 Trigger Feedback Regulation of Hypertrophy via Atrial Natriuretic Peptide in Cardiomyocytes

Banerjee¹,

Bandyopadhyay²

2014

Journal of Biological Chemistry

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Background: Altered annexin A6 expression is associated with several cardiovascular disorders, including myocyte hypertrophy, but precise functions of the protein remain elusive. Results: Dynamic association of annexin A6 with intracellular atrial natriuretic peptide precursor protects against adrenergic stimulation-induced hypertrophy of H9c2 cardiomyocytes. Conclusion: Annexin A6 negatively regulates hypertrophic progression of cardiomyocytes. Significance: Annexin A6 exhibits potential for antihypertrophic therapeutics.

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Section: Discussionmentioning

confidence: 99%

Section: Scrambshr and H9c2mentioning

confidence: 99%

Cytosolic Dynamics of Annexin A6 Trigger Feedback Regulation of Hypertrophy via Atrial Natriuretic Peptide in Cardiomyocytes

Banerjee¹,

Bandyopadhyay²

2014

Journal of Biological Chemistry

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“…Annexin A1 is intriguing because various annexins have been shown to regulate native Ca 2+ -activated Cl − channels. For example, annexin IV inhibits calmodulin-sensitive Cl − channels (37,38) as well as Ca 2+ -activated Cl − channels (39). In endothelial cells the annexin II-S100A10 complex might be involved in regulation of the swelling-activated Cl − channel (40) and cystic fibrosis transmembrane conductance regulator (41).…”

Section: Discussionmentioning

confidence: 99%

Anoctamin 1 (Tmem16A) Ca ² ⁺ -activated chloride channel stoichiometrically interacts with an ezrin–radixin–moesin network

Pérez‐Cornejo

Gokhale

Duran

et al. 2012

Proc. Natl. Acad. Sci. U.S.A.

114

139

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The newly discovered Ca 2+ -activated Cl − channel (CaCC), Anoctamin 1 (Ano1 or TMEM16A), has been implicated in vital physiological functions including epithelial fluid secretion, gut motility, and smooth muscle tone. Overexpression of Ano1 in HEK cells or Xenopus oocytes is sufficient to generate Ca 2+ -activated Cl − currents, but the details of channel composition and the regulatory factors that control channel biology are incompletely understood. We used a highly sensitive quantitative SILAC proteomics approach to obtain insights into stoichiometric protein networks associated with the Ano1 channel. These studies provide a comprehensive footprint of putative Ano1 regulatory networks. We find that Ano1 associates with the signaling/scaffolding proteins ezrin, radixin, moesin, and RhoA, which link the plasma membrane to the cytoskeleton with very high stoichiometry. Ano1, ezrin, and moesin/radixin colocalize apically in salivary gland epithelial cells, and overexpression of moesin and Ano1 in HEK cells alters the subcellular localization of both proteins. Moreover, interfering RNA for moesin modifies Ano1 current without affecting its surface expression level. Another network associated with Ano1 includes the SNARE and SM proteins VAMP3, syntaxins 2 and -4, and syntaxin-binding proteins munc18b and munc18c, which are integral to translocation of vesicles to the plasma membrane. A number of other regulatory proteins, including GTPases, Ca 2+ -binding proteins, kinases, and lipid-interacting proteins are enriched in the Ano1 complex. These data provide stoichiometrically prioritized information about mechanisms regulating Ano1 function and trafficking to polarized domains of the plasma membrane.calcium | interactome | cross-linker | apical targeting

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“…The final class was annexins, another structurally different family of calcium-dependent membrane-binding proteins (Rescher and Gerke, 2004;Gerke et al, 2005). Among these, Anxa6 containing eight repeating annexin motifs (Kaetzel et al, 1994;Naciff et al, 1996b) was isolated (Nos. 15 and 16) [ Fig.…”

Section: Proteins Preferentially Expressed In the Late Stagementioning

confidence: 99%

Proteomics analysis of the temporal changes in axonal proteins during maturation

Yamatani

Kawasaki

Mita

et al. 2010

Developmental Neurobiology

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After the initial primary projection, axons undergo various structural and functional changes to establish mature neural circuits. The changes in protein expression associated with this maturation were investigated in lateral olfactory tract axons using two-dimensional gel electrophoresis. The most prominent group upregulated during the period consisted of calcium-dependent membrane-binding proteins including VILIP1, neurocalcin delta, copine 6, and annexin A6 from three structurally different families. During maturation of primary cultured neurons, annexin A6 gradually became concentrated on the axon initial segment, and its overexpression significantly enhanced axon branching. On the other hand, overexpression of VILIP1 and neurocalcin delta reduced axon outgrowth and branching. The second group upregulated during axon maturation comprised tubulin- and microtubule-binding proteins including CRMP2, guanine deaminase, MAP1B, and fibronectin type3 SPRY domain-containing protein. Because the maturation of lateral olfactory axons involves massive extension of secondary collateral branches, the augmentation of these proteins during these stages may underlie the drastic restructuring of the axon cytoskeleton.

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Annexin VI isoforms are differentially expressed in mammalian tissues

Cited by 35 publications

References 33 publications

Cytosolic Dynamics of Annexin A6 Trigger Feedback Regulation of Hypertrophy via Atrial Natriuretic Peptide in Cardiomyocytes

Cytosolic Dynamics of Annexin A6 Trigger Feedback Regulation of Hypertrophy via Atrial Natriuretic Peptide in Cardiomyocytes

Anoctamin 1 (Tmem16A) Ca ² ⁺ -activated chloride channel stoichiometrically interacts with an ezrin–radixin–moesin network

Proteomics analysis of the temporal changes in axonal proteins during maturation

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Annexin VI isoforms are differentially expressed in mammalian tissues

Cited by 35 publications

References 33 publications

Cytosolic Dynamics of Annexin A6 Trigger Feedback Regulation of Hypertrophy via Atrial Natriuretic Peptide in Cardiomyocytes

Cytosolic Dynamics of Annexin A6 Trigger Feedback Regulation of Hypertrophy via Atrial Natriuretic Peptide in Cardiomyocytes

Anoctamin 1 (Tmem16A) Ca 2 + -activated chloride channel stoichiometrically interacts with an ezrin–radixin–moesin network

Proteomics analysis of the temporal changes in axonal proteins during maturation

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Anoctamin 1 (Tmem16A) Ca ² ⁺ -activated chloride channel stoichiometrically interacts with an ezrin–radixin–moesin network