K

Gerke, Wolfgang

doi:10.1007/978-3-322-82631-2_11

Cited by 18 publications

(27 citation statements)

References 0 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…However, upon transient transfection of annexin II constructs into CHO cells, we did not observe any stimulatory effect on the LDL or transferrin endocytosis, even when cotransfected with either the LDL or transferrin receptor. Since annexin II forms a stable heterotetrameric protein complex with p11, a protein of the S-100 family (47), limiting concentration of p11 protein in annexin II-transfected CHO cells could result in low amounts of active annexin II 2 p11 2 complex.…”

Section: Discussionmentioning

confidence: 99%

Annexin VI Stimulates Endocytosis and Is Involved in the Trafficking of Low Density Lipoprotein to the Prelysosomal Compartment

Grewal¹,

Heeren²,

Mewawala³

et al. 2000

Journal of Biological Chemistry

126

View full text Add to dashboard Cite

Annexins are calcium-binding proteins with a wide distribution in most polarized and nonpolarized cells that participate in a variety of membrane-membrane interactions. At the cell surface, annexin VI is thought to remodel the spectrin cytoskeleton to facilitate budding of coated pits. However, annexin VI is also found in late endocytic compartments in a number of cell types, indicating an additional important role at later stages of the endocytic pathway. Therefore overexpression of annexin VI in Chinese hamster ovary cells was used to investigate its possible role in endocytosis and intracellular trafficking of low density lipoprotein (LDL) and transferrin. While overexpression of annexin VI alone did not alter endocytosis and degradation of LDL, coexpression of annexin VI and LDL receptor resulted in an increase in LDL uptake with a concomitant increase of its degradation. Whereas annexin VI showed a wide intracellular distribution in resting Chinese hamster ovary cells, it was mainly found in the endocytic compartment and remained associated with LDL-containing vesicles even at later stages of the endocytic pathway. Thus, data presented in this study suggest that after stimulating endocytosis at the cell surface, annexin VI remains bound to endocytic vesicles to regulate entry of ligands into the prelysosomal compartment.Annexins are a family of highly conserved proteins, which are characterized by their Ca 2ϩ -dependent binding to phospholipids (1). Each annexin consists of a conserved core domain with four or eight repeats (70 amino acids) and a nonconserved, short, NH 2 -terminal domain. More than 10 different family members, several of which exist as multiple isoforms, have been described in higher vertebrates (2). Since annexins are expressed in many tissues and are located in the same cellular compartments, the understanding of the distinct physiological role of each annexin still remains elusive (1, 3). In recent years, the involvement of annexins in membrane traffic has emerged as one of their predominant functions (1, 4). Several annexins including annexin I, II, IV, VI, VII, and XIIIb have been directly implicated in different steps of the intracellular trafficking pathways (5-14) and, despite some controversy, essentially due to the variety of cells and antibodies used, they are all associated with the endocytic compartment.The enrichment of annexin VI in rat liver endosomes (12, 13), its polarized localization in the apical endosomes in rat hepatocytes (14) and WIF-B cells (15), and the colocalization with lgp120, a prelysosomal marker in normal rat kidney cells (15), indicate a potential role for annexin VI in the endocytic pathways of polarized and nonpolarized cells.In support of this hypothesis, annexin VI has been found to bind ␤-spectrin at the cell surface, which in turn recruits and activates a calpain-like protease. This cascade of events seems to open the actin-cortical cytoskeleton to facilitate the initial steps of endocytosis (16,17). The complexity of these interactions has recently...

show abstract

Section: Discussionmentioning

confidence: 99%

Annexin VI Stimulates Endocytosis and Is Involved in the Trafficking of Low Density Lipoprotein to the Prelysosomal Compartment

Grewal¹,

Heeren²,

Mewawala³

et al. 2000

Journal of Biological Chemistry

126

View full text Add to dashboard Cite

show abstract

“…Purification of S100A10 and Annexin2-Native A2t was purified from porcine intestine as previously described (35). S100A10 and Annexin2 were dissociated from the complex with 9 M urea.…”

Section: Methodsmentioning

confidence: 99%

Identification of an AHNAK Binding Motif Specific for the Annexin2/S100A10 Tetramer

Seranno

Benaud

Assard

et al. 2006

Journal of Biological Chemistry

View full text Add to dashboard Cite

The Annexin2 tetramer (A2t), which consists of two Annexin2 molecules bound to a S100A10 dimer, is implicated in membrane-trafficking events. Here, we showed using a yeast triple-hybrid experiment and in vitro binding assay that Annexin2 is required for strong binding of S100A10 to the C-terminal domain of the protein Ahnak. We also revealed that this effect involves only the Annexin2 N-terminal tail, which is implicated in S100A10/Annexin2 tetramerization. The minimal A2t binding motif (A2tBP1) in Ahnak was mapped to a 20-amino acid peptide, and this peptide is highly specific for A2t. We also identified a second A2t binding motif (A2tBP2) present in the N-terminal domain of Ahnak, which binds to A2t, albeit with less affinity. When overexpressed as an EGFP fusion protein in MDCK cells, A2tBPs cofractionate in a calcium-dependent manner and co-immunoprecipitate with S100A10 and Annexin2. In living cells, A2tBPs target EGFP to the cytoplasm as does Annexin2. In response to oxidative and mechanical stress, EGFP-A2tBPs relocalize within minutes to the plasma membrane; a behavior shared with Annexin2-GFP. These results suggest that the A2t complex exists within the cytoplasm of resting living cells and that its localization at the plasma membrane relies on cellular signaling. Together, our data demonstrate that A2tBP1 is a specific A2t complex binding domain and may be a powerful tool to help elucidate A2t structure and cellular functions.

show abstract

“…Anx2 1 is a major cytoplasmic substrate of the pp60 src tyrosine kinase (4)(5)(6). This protein is found either as a monomer (p36) or as a heterotetramer (p90) when two Anx2 molecules are associated with a dimer of p11, an S100-like protein devoid of tryptophan residues (7,8). It is likely involved in cellular events such as exo-and endocytosis (9)(10)(11)(12)(13)(14).…”

mentioning

confidence: 99%

Modulation by Ca²⁺ and by Membrane Binding of the Dynamics of Domain III of Annexin 2 (p36) and the Annexin 2−p11 Complex (p90): Implications for Their Biochemical Properties

et al. 2000

View full text Add to dashboard Cite

The modulation of the local structure and dynamics of domain III of annexin 2 (Anx2), in both the monomeric (p36) and heterotetrameric forms (p90), by calcium and by membrane binding was studied by time-resolved fluorescence intensity and anisotropy measurements of the single tryptophan residue (W212). The results yield the same dominant excited-state lifetime (1.4 ns) in both p36 and p90, suggesting that the conformation and environment of W212 are very similar. The fluorescence anisotropy decay data were analyzed by associative (two-dimensional) as well as nonassociative (one-dimensional) models. Although no statistical criterion is decisive for one model versus the other, only the associative model allows recovery of a physically relevant value of the Brownian rotational correlation of the protein. Using the associative model, a nanosecond flexibility is detectable in p90 but not in p36. When Ca(2+) binds in the millimolar concentration range to both forms of Anx2, a conformational change takes place leading to an increase of the major excited-state lifetime (2.6 ns) and to a suppression of the W212 local flexibility of p90. Binding to membranes of either p36 or p90 in the presence of Ca(2+) does not induce any conformational change other than that provoked by Ca(2+) binding alone. The W212 local flexibility in both proteins increases significantly, however, in their membrane-bound forms. In the presence of membranes, the conformation change of domain III in p90 displays a sensitivity to Ca(2+) 2 orders of magnitude higher than that of p36, reaching intracellular sub-micromolar concentration ranges. This higher Ca(2+) sensitivity correlates with the Ca(2+)-dependent membrane aggregation but not with their Ca(2+)-dependent binding to membranes. The significance of these structural and dynamical changes for the function of the protein is discussed.

show abstract

K

Cited by 18 publications

References 0 publications

Annexin VI Stimulates Endocytosis and Is Involved in the Trafficking of Low Density Lipoprotein to the Prelysosomal Compartment

Annexin VI Stimulates Endocytosis and Is Involved in the Trafficking of Low Density Lipoprotein to the Prelysosomal Compartment

Identification of an AHNAK Binding Motif Specific for the Annexin2/S100A10 Tetramer

Modulation by Ca²⁺ and by Membrane Binding of the Dynamics of Domain III of Annexin 2 (p36) and the Annexin 2−p11 Complex (p90): Implications for Their Biochemical Properties

Contact Info

Product

Resources

About

K

Cited by 18 publications

References 0 publications

Annexin VI Stimulates Endocytosis and Is Involved in the Trafficking of Low Density Lipoprotein to the Prelysosomal Compartment

Annexin VI Stimulates Endocytosis and Is Involved in the Trafficking of Low Density Lipoprotein to the Prelysosomal Compartment

Identification of an AHNAK Binding Motif Specific for the Annexin2/S100A10 Tetramer

Modulation by Ca2+ and by Membrane Binding of the Dynamics of Domain III of Annexin 2 (p36) and the Annexin 2−p11 Complex (p90): Implications for Their Biochemical Properties

Contact Info

Product

Resources

About

Modulation by Ca²⁺ and by Membrane Binding of the Dynamics of Domain III of Annexin 2 (p36) and the Annexin 2−p11 Complex (p90): Implications for Their Biochemical Properties