Identification of a putative effector protein for rab11 that participates in transferrin recycling

Zeng, Jin; Ren, Mindong; Gravotta, Diego; Lemos-Chiarandini, Carmen De; Lui, Michelle; Erdjument‐Bromage, Hediye; Tempst, Paul; Xu, Genxing; Shen, Tian Huai; Morimoto, Takashi; Adesnik, Milton; Sabatini, David D.

doi:10.1073/pnas.96.6.2840

Cited by 83 publications

(68 citation statements)

References 33 publications

(40 reference statements)

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“…11/Rab11BP, myosin Vb, Rip11, RCP, Rab11-FIP1, Rab11-FIP2, Rab11-FIP3, Rab11-FIP4 and Rab6IP1 Lapierre et al, 2001;Mammoto et al, 1999;Nizak et al, 2003;Prekeris et al, 2001;Prekeris et al, 2000;Wallace et al, 2002;Zeng et al, 1999). Rip11, RCP, Rab11-FIP2, Rab11-FIP1, Rab11-FIP3 and Rab11-FIP4 have been grouped into a family of proteins called the Rab11-FIPs.…”

Section: Discussionmentioning

confidence: 99%

The C2 domains of the class I Rab11 family of interacting proteins target recycling vesicles to the plasma membrane

Lindsay

McCaffrey

2004

Journal of Cell Science

104

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The Rab11 family of interacting proteins (Rab11-FIP) is a recently identified protein family composed of, to date, six members that interact with Rab11. They all share a highly homologous Rab11-binding domain (RBD) at their C-termini. However, apart from the RBD, they vary in their domain organization. Rab11-FIP3 and Rab11-FIP4 possess an ezrin-radixin-moesin (ERM) domain in their C-terminal half and EF hands in their N-terminal region. They have been termed class II Rab11-FIPs. The class I Rab11-FIPs, Rab coupling protein (RCP), Rip11 and Rab11-FIP2, each have a C2 phospholipid-binding domain near their N-termini. Although they are still membrane associated, truncation mutants of the class I Rab11-FIPs that lack their C2 domains display an altered subcellular distribution in vivo, indicating that this domain plays an important role in specifying their correct intracellular localization. To determine the phospholipids to which they bind, a protein phospholipid overlay assay was performed. Our results indicate that the class-I Rab11-FIPs bind preferentially to phosphatidylinositol-(3,4,5)-trisphosphate [PtdIns(3,4,5)P3] and the second messenger phosphatidic acid. Stimulation of PtdIns(3,4,5)P3 or phosphatidic acid synthesis results in the translocation of the Rab11-FIPs from a perinuclear location to the periphery of the cell. By contrast, the transferrin receptor does not translocate to the plasma membrane under these conditions. This translocation is dependent on the presence of the C2 domain, because class I Rab11-FIP green-fluorescent-protein fusions that lack the C2 domain cannot translocate to the plasma membrane. We propose that the C2 domains of the class I Rab11-FIPs function to target these proteins to `docking sites' in the plasma membrane that are enriched in PtdIns(3,4,5)P3 and phosphatidic acid.

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Section: Discussionmentioning

confidence: 99%

The C2 domains of the class I Rab11 family of interacting proteins target recycling vesicles to the plasma membrane

Lindsay

McCaffrey

2004

Journal of Cell Science

104

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“…Rab11BP/rabphilin-11 (12,14,15). It will be interesting to see whether these proteins can actually co-bind to Rab11/25 with either Eferin or Rips, perhaps forming signaling complexes that regulate transport vesicle trafficking.…”

Section: Fig 3 Identification Of the Rbd11 Conserved In Rip Andmentioning

confidence: 99%

“…During the last few years several Rab11/25-interacting proteins have been identified, including Rab11BP/rabphilin-11, Rip11, nRip11, and myosin Vb (12)(13)(14)(15). However, the mechanisms of their function, as well as molecular aspects of their interactions with Rab11, remain to be fully understood.…”

mentioning

confidence: 99%

Identification of a Novel Rab11/25 Binding Domain Present in Eferin and Rip Proteins

Prekeris¹,

Davies²,

Scheller³

2001

Journal of Biological Chemistry

103

123

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Rab11, a low molecular weight GTP-binding protein, has been shown to play a key role in a variety of cellular processes, including endosomal recycling, phagocytosis, and transport of secretory proteins from the trans-Golgi network. In this study we have described a novel Rab11 effector, EF-hands-containing Rab11-interacting protein (Eferin). In addition, we have identified a 20-amino acid domain that is present at the C terminus of Eferin and other Rab11/25-interacting proteins, such as Rip11 and nRip11. Using biochemical techniques we have demonstrated that this domain is necessary and sufficient for Rab11 binding in vitro and that it is required for localization of Rab11 effector proteins in vivo. The data suggest that various Rab effectors compete with each other for binding to Rab11/25 possibly accounting for the diversity of Rab11 functions.

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“…The molecular mechanisms by which Rab11a performs its regulatory role are still poorly understood. Previous studies have identified a number of Rab11a interacting proteins, including myosin Vb , Rab11-binding protein/Rabphilin 11 (Mammoto et al, 1999;Zeng et al, 1999), and a group of Rab11-family interacting proteins (Rab11-FIPs) such as pp75/Rip11, Rab11-FIP1, Rab11-FIP2, Rab11-FIP3, Rab11-FIP4, and Rab-coupling protein (Prekeris et al, 2000;Hales et al, 2001;Lindsay et al, 2002;Wallace et al, 2002). Among these Rab11 interacting proteins, myosin Vb and Rab11-FIP2 are of particular interest because both proteins associate with each other and Rab11a Hales et al, 2002).…”

mentioning

confidence: 99%

Rab11-Family Interacting Protein 2 and Myosin Vb Are Required for CXCR2 Recycling and Receptor-mediated Chemotaxis

Fan

Lapierre

Goldenring

et al. 2004

MBoC

127

130

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Agonist-stimulated internalization followed by recycling to the cell membrane play an important role in fine-tuning the activity of chemokine receptors. Because the recycling of chemokine receptors is critical for the reestablishment of the cellular responsiveness to ligand, it is crucial to understand the mechanisms underlying the receptor recycling and resensitization. In the present study, we have demonstrated that the chemokine receptor CXCR2 associated with myosin Vb and Rab11-family interacting protein 2 (FIP2) in a ligand-dependent manner. Truncation of the C-terminal domain of the receptor did not affect the association, suggesting that the interactions occur upstream of the C terminus of CXCR2. After ligand stimulation, the internalized CXCR2 colocalized with myosin Vb and Rab11-FIP2 in Rab11a-positive vesicles. The colocalization lasted for ϳ2 h, and little colocalization was observed after 4 h of ligand stimulation. CXCR2 also colocalized with myosin Vb tail or Rab11-FIP2 (129 -512), the N-terminal-truncated mutants of myosin Vb and Rab11-FIP2, respectively, but in a highly condensed manner. Expression of the enhanced green fluorescent protein-tagged myosin Vb tail significantly retarded the recycling and resensitization of CXCR2. CXCR2 recycling was also reduced by the expression Rab11-FIP2 (129 -512). Moreover, expression of the myosin Vb tail reduced CXCR2-and CXCR4-mediated chemotaxis. These data indicate that Rab11-FIP2 and myosin Vb regulate CXCR2 recycling and receptor-mediated chemotaxis and that passage of internalized CXCR2 through Rab11a-positive recycling system is critical for physiological response to a chemokine. INTRODUCTIONChemokine receptors belong to the large family of seventransmembrane G protein-coupled receptors (GPCRs) that function in immune and inflammatory response by regulating the activation and migration of leukocytes, immune cell development, and angiogenesis (Nagasawa et al., 1996;Luster 1998;Belperio et al., 2000;Murphy et al., 2000;Zlotnik and Yoshie, 2000). Some of them (e.g., CCR5 and CXCR4) participate in HIV infection of CD4 ϩ T lymphocytes as coreceptors (Berger et al., 1999). Ligand binding to the chemokine receptors triggers various signaling cascades, including activation of G proteins, phosphotidylinositol 3-kinase, Janus kinase/signal transducers and activators of transcription proteins, the Rho-p160 ROCK axis, and the MAPK pathway (Wu et al., 1993;Ganju et al., 1998;Mellado et al., 1998;Vicente-Manzanares et al., 1999;Vicente-Manzanares et al., 2002). Chemokine activation of these intracellular signals is often accompanied by chemokine receptor internalization and trafficking back to the cell membrane. The intracellular trafficking of chemokine receptors controls their activities, and the balance between the chemokine receptor recycling and degradation dictates the leukocyte responsiveness to chemokines (Sabroe et al., 1997;Asagoe et al., 1998;Khandaker et al., 1998;Mack et al., 1998).Ligand stimulated chemokine receptor internalization can be accomplished ...

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Identification of a putative effector protein for rab11 that participates in transferrin recycling

Cited by 83 publications

References 33 publications

The C2 domains of the class I Rab11 family of interacting proteins target recycling vesicles to the plasma membrane

The C2 domains of the class I Rab11 family of interacting proteins target recycling vesicles to the plasma membrane

Identification of a Novel Rab11/25 Binding Domain Present in Eferin and Rip Proteins

Rab11-Family Interacting Protein 2 and Myosin Vb Are Required for CXCR2 Recycling and Receptor-mediated Chemotaxis

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