EH Domain Proteins Pan1p and End3p Are Components of a Complex That Plays a Dual Role in Organization of the Cortical Actin Cytoskeleton and Endocytosis in <i>Saccharomyces cerevisiae</i>

Tang, Hsin‐Yao; Munn, Alan Leslie; Cai, Meng

doi:10.1128/mcb.17.8.4294

Cited by 121 publications

(164 citation statements)

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“…Immunoprecipitation and immunoblotting followed the published procedure (Tang et al, 1997) with slight modifications. The beadsconjugated anti-hemagglutinin (HA) or anti-Myc polyclonal antibodies (Santa Cruz Biotechnology, Santa Cruz, CA) were used to immunoprecipitate epitope-tagged proteins.…”

Section: Protein Extraction Immunoprecipitation and Immunoblottingmentioning

confidence: 99%

“…Yeast extracts were prepared by either glass beads method or trichloroacetic acid (TCA) precipitation method as described previously (Tang et al, 1997;Huang et al, 2003). Immunoprecipitation and immunoblotting followed the published procedure (Tang et al, 1997) with slight modifications.…”

Section: Protein Extraction Immunoprecipitation and Immunoblottingmentioning

confidence: 99%

“…The essential yeast protein Pan1p plays a central role in coat formation by interacting with multiple coat proteins, including End3p, Sla1/2p, Yap1801/2p, and Ent1/2p (Tang et al, 1997;Wendland and Emr, 1998;Wendland et al, 1999;Tang et al, 2000;Toshima et al, 2007). Pan1p also possesses the ability to activate the Arp2/3 complex, and may cooperate with other nucleation-promoting factors, such as Las17p and Myo5p, to initiate actin assembly at endocytic sites (Duncan et al, 2001;Sun et al, 2006).…”

Section: Introductionmentioning

confidence: 99%

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Scd5p Mediates Phosphoregulation of Actin and Endocytosis by the Type 1 Phosphatase Glc7p in Yeast

Zeng

Neo

Wang

et al. 2007

MBoC

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Pan1p plays essential roles in both actin and endocytosis in yeast. It interacts with, and regulates the function of, multiple endocytic proteins and actin assembly machinery. Phosphorylation of Pan1p by the kinase Prk1p down-regulates its activity, resulting in disassembly of the endocytic vesicle coat complex and termination of vesicle-associated actin polymerization. In this study, we focus on the mechanism that acts to release Pan1p from phosphorylation inhibition. We show that Pan1p is dephosphorylated by the phosphatase Glc7p, and the dephosphorylation is dependent on the Glc7p-targeting protein Scd5p, which itself is a phosphorylation target of Prk1p. Scd5p links Glc7p to Pan1p in two ways: directly by interacting with Pan1p and indirectly by interacting with the Pan1p-binding protein End3p. Depletion of Glc7p from the cells causes defects in cell growth, actin organization, and endocytosis, all of which can be partially suppressed by deletion of the PRK1 gene. These results suggest that Glc7p antagonizes the activity of the Prk1p kinase in regulating the functions of Pan1p and possibly other actin-and endocytosis-related proteins.

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Section: Protein Extraction Immunoprecipitation and Immunoblottingmentioning

confidence: 99%

Section: Protein Extraction Immunoprecipitation and Immunoblottingmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Scd5p Mediates Phosphoregulation of Actin and Endocytosis by the Type 1 Phosphatase Glc7p in Yeast

Zeng

Neo

Wang

et al. 2007

MBoC

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“…In yeast, mutations in actin or fimbrin inhibit endocytosis (Kubler and Riezman, 1993). Additionally, genetic screens for mutants affecting endocytosis have revealed mutations in several genes that disrupt both endocyThis article was published online ahead of print in MBC in Press (http://www.molbiolcell.org/cgi/doi/10.1091/mbc.E04 -11-1014) on March 16, 2005. tosis and actin organization (Benedetti et al, 1994;Munn et al, 1995;Tang et al, 1997). However, some yeast mutants that disrupt actin organization have no effect on endocytosis (Riezman et al, 1997), and some suppressors of an endocytosis mutant that also affects actin organization (end5) can rescue one or the other phenotype, but not both, suggesting that they are separable (Riezman et al, 1997).…”

Section: Introductionmentioning

confidence: 99%

“…© 2005 by The American Society for Cell Biology tosis and actin organization (Benedetti et al, 1994;Munn et al, 1995;Tang et al, 1997). However, some yeast mutants that disrupt actin organization have no effect on endocytosis (Riezman et al, 1997), and some suppressors of an endocytosis mutant that also affects actin organization (end5) can rescue one or the other phenotype, but not both, suggesting that they are separable (Riezman et al, 1997).…”

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confidence: 99%

CART: An Hrs/Actinin-4/BERP/Myosin V Protein Complex Required for Efficient Receptor Recycling

Yan

Wei

Kujala

et al. 2005

MBoC

113

121

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Altering the number of surface receptors can rapidly modulate cellular responses to extracellular signals. Some receptors, like the transferrin receptor (TfR), are constitutively internalized and recycled to the plasma membrane. Other receptors, like the epidermal growth factor receptor (EGFR), are internalized after ligand binding and then ultimately degraded in the lysosome. Routing internalized receptors to different destinations suggests that distinct molecular mechanisms may direct their movement. Here, we report that the endosome-associated protein hrs is a subunit of a protein complex containing actinin-4, BERP, and myosin V that is necessary for efficient TfR recycling but not for EGFR degradation. The hrs/actinin-4/BERP/myosin V (CART [cytoskeleton-associated recycling or transport]) complex assembles in a linear manner and interrupting binding of any member to its neighbor produces an inhibition of transferrin recycling rate. Disrupting the CART complex results in shunting receptors to a slower recycling pathway that involves the recycling endosome. The novel CART complex may provide a molecular mechanism for the actin-dependence of rapid recycling of constitutively recycled plasma membrane receptors. INTRODUCTIONEndocytosis is required for the uptake of essential nutrients from the extracellular environment as well as for retrieval of proteins and lipids that are added to the plasma membrane during fusion of regulated and constitutive secretory vesicles (De Camilli and Takei, 1996;Koenig and Ikeda, 1996;Robinson et al., 1996;Mukherjee et al., 1997;Schmid, 1997;Betz and Angleson, 1998;Koenig et al., 1998;Stoorvogel, 1998;D'Hondt et al., 2000;Gruenberg, 2001). The endocytic pathway can be separated into numerous stages based on the movement of cargo and the identification of morphologically defined compartments (De Camilli and Takei, 1996;Koenig and Ikeda, 1996;Robinson et al., 1996;Mukherjee et al., 1997;Schmid, 1997;Betz and Angleson, 1998;Koenig et al., 1998;Stoorvogel, 1998;D'Hondt et al., 2000;Gruenberg, 2001). Early events in the endocytic process include membrane invagination and vesicle budding from the plasma membrane, formation of transport vesicles, and fusion with early endosomes. Later events include cargo sorting, and additional transport/fusion steps, including those responsible for transport to the lysosome for degradation, and those responsible for recycling back to various compartments (De Camilli and Takei, 1996;Koenig and Ikeda, 1996;Robinson et al., 1996;Mukherjee et al., 1997;Schmid, 1997;Betz and Angleson, 1998;Koenig et al., 1998;Stoorvogel, 1998;D'Hondt et al., 2000;Gruenberg, 2001). Although much progress has been made in elucidating the molecular processes involved in early endocytic events, such as those involved in the genesis of clathrin-coated endocytic transport vesicles, an equally clear understanding of later events remains elusive.The early endosome is a crucial point in the endocytic pathway to sort cargo for transport to late endosomes for eventual degradation in the...

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The yeast endocytic membrane transport system

Munn

2000

Microsc. Res. Tech.

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Progress has been made recently in visualizing the structures and organelles responsible for endocytic membrane traffic from the cell surface to the lysosome‐like vacuole in Saccharomyces cerevisiae. This, together with the recent discovery of several new membrane trafficking pathways connecting these organelles, has led to a quantum leap in our understanding of the S. cerevisiae endocytic pathway. We now know that although the cortical actin cytoskeleton is required for the internalization step of endocytosis, the internalization event occurs at furrow‐like invaginations of the plasma membrane, which are distinct from cortical actin patches. Internalized material is taken into the cell in the form of small (30–50 nm diameter) vesicles and delivered to tubulo‐vesicular early endosomes at the cell periphery. Subsequently, the internalized material arrives in multivesicular late endosomes adjacent to the vacuole. Recent microscopy evidence suggests that transfer from late endosomes to the vacuole may involve direct fusion of late endosomes with the vacuole. The visualization of the S. cerevisiae endocytic pathway has revealed similarities to endocytic pathways visualized in higher eukaryotes. Microsc. Res. Tech. 51:547–562, 2000. © 2000 Wiley‐Liss, Inc.

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EH Domain Proteins Pan1p and End3p Are Components of a Complex That Plays a Dual Role in Organization of the Cortical Actin Cytoskeleton and Endocytosis in Saccharomyces cerevisiae

Cited by 121 publications

References 50 publications

Scd5p Mediates Phosphoregulation of Actin and Endocytosis by the Type 1 Phosphatase Glc7p in Yeast

Scd5p Mediates Phosphoregulation of Actin and Endocytosis by the Type 1 Phosphatase Glc7p in Yeast

CART: An Hrs/Actinin-4/BERP/Myosin V Protein Complex Required for Efficient Receptor Recycling

The yeast endocytic membrane transport system

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