Rab4 affects both recycling and degradative endosomal trafficking

McCaffrey, Mary W.; Bielli, Anna; Cantalupo, Giuseppina; Mora, Sílvia; Roberti, Vera; Santillo, Mariarosaria; Drummond, Frances J.; Bucci, Cecilia

doi:10.1016/s0014-5793(01)02359-6

Cited by 153 publications

(142 citation statements)

References 47 publications

Supporting

Mentioning

125

Contrasting

Order By: Relevance

“…These results contrast with studies of Rab4, a protein associated with recycling from basolateral early endosomes (Sheff et al, 1999) in which expression of a GTP-binding mutant decreased the rate of Tf recycling (McCaffrey et al, 2001). Although the inhibition of recycling induced by expression of the mutant Rab4 indicates that Rab4 is necessary for recycling, the enhanced recycling induced by expression of mutant Rab10 suggests that Rab10 somehow negatively regulates recycling from basolateral sorting endosomes.…”

Section: Rab10 Mediates Transport From Basolateral Sorting Endosomes contrasting

confidence: 85%

“…The corresponding mutations in Ras, Rab7, Rab8, Rab11a, and Rab25 have been shown to decrease the affinity of the protein for GTP, resulting in the accumulation of a GDP-bound form (Feig and Cooper, 1988;Peranen et al, 1996;Bucci et al, 2000;Wang et al, 2000). This mutation frequently results in a protein with dominant-negative effects on Rab function; overexpression has been found to alter the function of Rab8 (Moritz et al, 2001) and yeast Sec4p (Walworth et al, 1989), as well as Rab4 (McCaffrey et al, 2001), Rab5 , Rab7 (Feng et al, 1995;Bucci et al, 2000), Rab11 (Ullrich et al, 1996;Wang et al, 2000a), Rab14 (Jununtula et al, 2004), and Rab15 (Zuk and Elferink, 2000). A second mutant was also created, encoding a change from glutamine into leucine at position 68 (Q68L).…”

Section: Mutations In the Gtp-binding And Gtp-hydrolysis Domains Altementioning

confidence: 99%

See 1 more Smart Citation

Rab10 Regulates Membrane Transport through Early Endosomes of Polarized Madin-Darby Canine Kidney Cells

Babbey

Ahktar

Wang

et al. 2006

MBoC

155

129

View full text Add to dashboard Cite

Section: Rab10 Mediates Transport From Basolateral Sorting Endosomes contrasting

confidence: 85%

Section: Mutations In the Gtp-binding And Gtp-hydrolysis Domains Altementioning

confidence: 99%

Rab10 Regulates Membrane Transport through Early Endosomes of Polarized Madin-Darby Canine Kidney Cells

Babbey

Ahktar

Wang

et al. 2006

MBoC

155

129

View full text Add to dashboard Cite

“…Our cloned Rab4a sequence was identical to the reported rat Rab4a sequence in the NCBI data base (accession number P05714) with the exception of two differences: Q47S and T75R. These two amino acids in our sequence (Ser 47 ) and (Arg 75 ) are conserved in the mouse and human sequences reported in the NCBI data base (accession numbers NP_033029 and NP_004569, respectively). Therefore, these two differences probably correspond to sequencing errors in the previously reported rat sequence.…”

Section: Methodssupporting

confidence: 67%

Local Control of AMPA Receptor Trafficking at the Postsynaptic Terminal by a Small GTPase of the Rab Family

Gerges

Backos

Esteban

2004

Journal of Biological Chemistry

131

139

View full text Add to dashboard Cite

The delivery of neurotransmitter receptors into the synaptic membrane is essential for synaptic function and plasticity. However, the molecular mechanisms of these specialized trafficking events and their integration with the intracellular membrane transport machinery are virtually unknown. Here, we have investigated the role of the Rab family of membrane sorting proteins in the late stages of receptor trafficking into the postsynaptic membrane. We have identified Rab8, a vesicular transport protein associated with trans-Golgi network membranes, as a critical component of the cellular machinery that delivers AMPA-type glutamatergic receptors (AMPARs) into synapses. Using electron microscopic techniques, we have found that Rab8 is localized in close proximity to the synaptic membrane, including the postsynaptic density. Electrophysiological studies indicated that Rab8 is necessary for the synaptic delivery of AMPARs during plasticity (long-term potentiation) and during constitutive receptor cycling. In addition, Rab8 is required for AMPAR delivery into the spine surface, but not for receptor transport from the dendritic shaft into the spine compartment or for delivery into the dendritic surface. Therefore, Rab8 specifically drives the local delivery of AMPARs into synapses. These results demonstrate a new role for the cellular secretory machinery in the control of synaptic function and plasticity directly at the postsynaptic membrane.

show abstract

“…For example, rab5a is present on endosomes, is involved in endosome-endosome fusion (Gournier et al, 1998), in linking early endosomes to microtubules, and in minus-end-directed movement (Nielsen et al, 1999), although rab5a has not yet been demonstrated to interact with any motor protein. Rab 4 and rab 11 are endosome-associated proteins thought to be involved in recycling (Van Der Sluijs et al, 1991;McCaffrey et al, 2001;Peden et al, 2004) but their precise roles and which of the many possible effectors are relevant for this function remains unclear (Nagelkerken et al, 2000;Cormont et al, 2001;van der Sluijs et al, 2001;Fouraux et al, 2004;Peden et al, 2004). The present data suggest that hrs may link endosomes to actin through actinin-4, BERP, and myosin Vb.…”

Section: Discussionmentioning

confidence: 60%

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

Yan

Wei

Kujala

et al. 2005

MBoC

115

121

View full text Add to dashboard Cite

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...

show abstract

Rab4 affects both recycling and degradative endosomal trafficking

Cited by 153 publications

References 47 publications

Rab10 Regulates Membrane Transport through Early Endosomes of Polarized Madin-Darby Canine Kidney Cells

Rab10 Regulates Membrane Transport through Early Endosomes of Polarized Madin-Darby Canine Kidney Cells

Local Control of AMPA Receptor Trafficking at the Postsynaptic Terminal by a Small GTPase of the Rab Family

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

Contact Info

Product

Resources

About