Rab11‐FIP3 Is Critical for the Structural Integrity of the Endosomal Recycling Compartment

Horgan, Conor P.; Oleksy, Arkadiusz; Zhdanov, Alexander V.; Lall, Patrick; White, Ian J.; Khan, Amir R.; Futter, Clare E.; McCaffrey, John G.; McCaffrey, Mary W.

doi:10.1111/j.1600-0854.2007.00543.x

Cited by 66 publications

(95 citation statements)

References 61 publications

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“…In FIP3-depleted cells, ASAP1 was still at the perinuclear region. Rab11 was dispersed throughout the cell as previously reported (Horgan et al, 2007), but some Rab11 was present with ASAP1( Figure 10B, inset 1). Rab11 on the vesicles throughout the cell rarely colocalized with ASAP1 ( Figure 10B, inset 2).…”

supporting

confidence: 60%

“…This effect is dependent on the ability to bind to Rab11 Horgan et al, 2004). In contrast, depletion of FIP3 induces loss of the perinuclear recycling endosomal compartment (Horgan et al, 2007). Based on these results, FIP3 has been proposed to be a critical regulator of the recycling endosome together with Rab11.…”

Section: Introductionmentioning

confidence: 71%

“…Rab11 and Arf5/6 bind to C-terminal end and C-terminal half of the coiled-coil domain, respectively (Prekeris et al, 2001;Shiba et al, 2006;Schonteich et al, 2007). The domain also mediates homodimerization and heterodimer formation with other FIPs, which also contain coiled-coil domain in their C-terminal region (Wallace et al, 2002;Eathiraj et al, 2006;Shiba et al, 2006;Horgan et al, 2007). We found the ASAP1 BAR domain binds to the middle of the FIP3 coiled-coil domain.…”

Section: Discussionmentioning

confidence: 88%

“…FIP3 is involved in the accumulation of recycling endosome in the pericentrosomal region (Horgan et al, 2007). To define the function of ASAP1 in the endocytic recycling compartment, endogenous ASAP1 or FIP3 was depleted using siRNAs in HeLa cells.…”

Section: Asap1 and Fip3 Are Required For Perinuclear Localization Of mentioning

confidence: 99%

“…FIP3, like other members of the FIP family, has a Rab11-binding site at its C-terminus (Prekeris, 2003). FIP3 and its closest homolog FIP4 function to maintain the integrity of recycling endosomes and to regulate cytokinesis during interphase and mitotic phase, respectively Wilson et al, 2005;Horgan et al, 2007). Overexpression of FIP3 or FIP4 causes accumulation of recycling endosome at the perinuclear region.…”

mentioning

confidence: 99%

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Arf GTPase-activating Protein ASAP1 Interacts with Rab11 Effector FIP3 and Regulates Pericentrosomal Localization of Transferrin Receptor–positive Recycling Endosome

Inoue

Prekeris

et al. 2008

MBoC

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ADP-ribosylation factors (Arfs) and Arf GTPase-activating proteins (GAPs) are key regulators of membrane trafficking and the actin cytoskeleton. The Arf GAP ASAP1 contains an N-terminal BAR domain, which can induce membrane tubulation. Here, we report that the BAR domain of ASAP1 can also function as a protein binding site. Two-hybrid screening identified FIP3, which is a putative Arf6-and Rab11-effector, as a candidate ASAP1 BAR domain-binding protein. Both coimmunoprecipitation and in vitro pulldown assays confirmed that ASAP1 directly binds to FIP3 through its BAR domain. ASAP1 formed a ternary complex with Rab11 through FIP3. FIP3 binding to the BAR domain stimulated ASAP1 GAP activity against Arf1, but not Arf6. ASAP1 colocalized with FIP3 in the pericentrosomal endocytic recycling compartment. Depletion of ASAP1 or FIP3 by small interfering RNA changed the localization of transferrin receptor, which is a marker of the recycling endosome, in HeLa cells. The depletion also altered the trafficking of endocytosed transferrin. These results support the conclusion that ASAP1, like FIP3, functions as a component of the endocytic recycling compartment. INTRODUCTIONArf family GTP-binding proteins and their GTPase-activating proteins (Arf GAPs) play crucial roles for membrane traffic and actin remodeling (D'Souza-Schorey and Chavrier, 2006;Gillingham and Munro, 2007). Arf GAPs share the same catalytic domain, the Arf GAP domain, which is responsible for GTP hydrolysis. In humans, 31 genes encoding proteins with Arf GAP domains have been found. They are classified into several subfamilies based on their domain structures Inoue and Randazzo, 2007). Three subfamilies, ArfGAPs, SMAPs, and GITs, have an Arf GAP domain at the N-terminus of the molecules. In contrast, the others, which are called AZAP-family Arf GAPs, contain an Arf GAP domain following a pleckstrin homology (PH) domain in the middle of the protein. They are subdivided into four subfamilies, ASAPs, ACAPs, ARAPs, and AGAPs.ASAP1 is one of the best-characterized Arf GAPs. In addition to PH and Arf GAP domains, ASAP1 contains an N-terminal Bin, Amphiphysin, and Rvs167/Rvs161 (BAR) domain and, in the C-terminal half of the protein, a proline (Pro)-rich domain and Src homology 3 (SH3) domain. Other ASAP isoforms, ASAP2 and ASAP3, have similar domain structures and high homology, especially in the Arf GAP domains, although ASAP3 lacks C-terminal SH3 domain (Ha et al., 2008). Through its Pro-rich and SH3 domains, ASAP1 interacts with a number of proteins, which are mainly adhesion-and actin cytoskeleton-related proteins including Src, focal adhesion kinase (FAK), Crk/CrkL, and cortactin (Brown et al., 1998;Liu et al., 2002;Oda et al., 2003;Onodera et al., 2005;Bharti et al., 2007). ASAP1 is a component of three integrated membrane/actin cytoskeleton structures: focal adhesions, circular dorsal ruffles (CDRs) and invadopodia/podosomes. ASAP1 associates with focal adhesions in fibroblasts . The focal adhesion localization depends on the interaction of ASAP1 with FA...

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supporting

confidence: 60%

Section: Introductionmentioning

confidence: 71%

Section: Discussionmentioning

confidence: 88%

Section: Asap1 and Fip3 Are Required For Perinuclear Localization Of mentioning

confidence: 99%

mentioning

confidence: 99%

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Arf GTPase-activating Protein ASAP1 Interacts with Rab11 Effector FIP3 and Regulates Pericentrosomal Localization of Transferrin Receptor–positive Recycling Endosome

Inoue

Prekeris

et al. 2008

MBoC

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Survey of the year 2007 commercial optical biosensor literature

Rich

Myszka

2008

J of Molecular Recognition

166

121

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In 2007, 1179 papers were published that involved the application of optical biosensors. Reported developments in instrument hardware, assay design, and immobilization chemistry continue to improve the technology's throughput, sensitivity, and utility. Compared to recent years, the widest range of platforms, both traditional format and array-based, were used. However, as in the past, we found a disappointingly low percentage of well-executed experiments and thoughtful data interpretation. We are alarmed by the high frequency of suboptimal data and over-interpreted results in the literature. Fortunately, learning to visually recognize good--and more importantly, bad--data is easy. Using examples from the literature, we outline several features of biosensor responses that indicate experimental artifacts versus actual binding events. Our goal is to have everyone, from benchtop scientists to project managers and manuscript reviewers, become astute judges of biosensor results using nothing more than their eyes.

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ADNP differentially interact with genes/proteins in correlation with aging: a novel marker for muscle aging

Kapitansky

Gozes

2019

GeroScience

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Activity-dependent neuroprotective protein (ADNP) is essential for embryonic development with ADNP mutations leading to syndromic autism, coupled with intellectual disabilities and motor developmental delays. Here, mining human muscle gene-expression databases, we have investigated the association of ADNP transcripts with muscle aging. We discovered increased ADNP and its paralogue ADNP2 expression in the vastus lateralis muscle of aged compared to young subjects, as well as altered expression of the ADNP and the ADNP2 genes in bicep brachii muscle of elderly people, in a sex-dependent manner. Prolonged exercise resulted in decreased ADNP expression, and increased ADNP2 expression in an age-dependent manner in the vastus lateralis muscle. ADNP expression level was further correlated with 49 genes showing agedependent changes in muscle transcript expression. A high degree of correlation with ADNP was discovered for 24 genes with the leading gene/protein being NMNAT1 (nicotinamide nucleotide adenylyl transferase 1). Looking at correlations differentiating the young and the old muscles and comparing protein interactions revealed an association of ADNP with the cell division cycle 5-like protein (CDC5L), and an aging-muscle-related interactive pathway in the vastus lateralis. In the bicep brachii, very high correlation was detected with genes associated with immune functions as well as mitochondrial structure and function among others. Taken together, the results suggest a direct association of ADNP with muscle strength and implicate ADNP fortification in the protection against age-associated muscle wasting.

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Rab11‐FIP3 Is Critical for the Structural Integrity of the Endosomal Recycling Compartment

Cited by 66 publications

References 61 publications

Arf GTPase-activating Protein ASAP1 Interacts with Rab11 Effector FIP3 and Regulates Pericentrosomal Localization of Transferrin Receptor–positive Recycling Endosome

Arf GTPase-activating Protein ASAP1 Interacts with Rab11 Effector FIP3 and Regulates Pericentrosomal Localization of Transferrin Receptor–positive Recycling Endosome

Survey of the year 2007 commercial optical biosensor literature

ADNP differentially interact with genes/proteins in correlation with aging: a novel marker for muscle aging

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