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The critically acclaimed laboratory standard for more than forty years, Methods in Enzymology is one of the most highly respected publications in the field of biochemistry. Since 1955, each volume has been eagerly awaited, frequently consulted, and praised by researchers and reviewers alike. Now with over 400 volumes (all of them still in print), the series contains much material still relevant today-truly an essential publication for researchers in all fields of life sciences. Methods in Enzymology is now available online at ScienceDirect -
full-text online of volumes 1 onwards. For more information about
the Elsevier Book Series on ScienceDirect Program, please
visit:
The critically acclaimed laboratory standard for more than 40 years, "Methods in Enzymology" is one of the most highly respected publications in the field of biochemistry. Since 1955, each volume has been eagerly awaited, frequently consulted, and praised by researchers and reviewers alike. Now with over 400 volumes (all of them still in print), the series contains much material still relevant today-truly an essential publication for researchers in all fields of life sciences. "Methods in Enzymology" is now available online at ScienceDirect
- full-text online of volume 1 onward. For more information about
the Elsevier Book Series on ScienceDirect Program, please
visit:
The Ras superfamily (>150 human members) encompasses Ras GTPases
involved in cell proliferation, Rho GTPases involved in regulating
the cytoskeleton, Rab GTPases involved in membrane targeting/fusion
and a group of GTPases including Sar1, Arf, Arl and dynamin
involved in vesicle budding/fission. These GTPases act as molecular
switches and their activities are controlled by a large number of
regulatory molecules that affect either GTP loading (guanine
nucleotide exchange factors or GEFs) or GTP hydrolysis (GTPase
activating proteins or GAPs). In their active state, they interact
with a continually increasing, functionally complex array of
downstream effectors.
The Ras superfamily (>150 human members) encompasses Ras GTPases
involved in cell proliferation, Rho GTPases involved in regulating
the cytoskeleton, Rab GTPases involved in membrane targeting/fusion
and a group of GTPases including Sar1, Arf, Arl and dynamin
involved in vesicle budding/fission. These GTPases act as molecular
switches and their activities are controlled by a large number of
regulatory molecules that affect either GTP loading (guanine
nucleotide exchange factors or GEFs) or GTP hydrolysis (GTPase
activating proteins or GAPs). In their active state, they interact
with a continually increasing, functionally complex array of
downstream effectors.
Rab GTPases now comprise a family of >63 members. They are
emerging as the key hub element controlling the membrane
architecture of eukaryotic cells. They are intimately involved in
vesicle targeting and fusion in both the endocytic and exocytic
pathways and direct the assembly and disassembly of protein
complexes that include regulators (GEFs and GAPs), effectors
(tethers/motors) and fusion components (SNAREs) that control
membrane targeting and fusion. During the last 3 years the field
has virtually exploded with the identification and characterization
of many new Rab proteins and their effectors.
General Description of the Volume:
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