The Experts below are selected from a list of 116469 Experts worldwide ranked by ideXlab platform
Mathew E. Sowa - One of the best experts on this subject based on the ideXlab platform.
-
an fts hook p107fhip complex interacts with and promotes endosomal clustering by the homotypic vacuolar protein sorting complex
Molecular Biology of the Cell, 2008Co-Authors: Mathew E. Sowa, Jing Chen, Steven P. Gygi, Wade J HarperAbstract:Fused Toes (FTS) is a member of a small group of inactive variant E2 ubiquitin-conjugating enzyme domain-containing proteins of unknown function. Through proteomic analysis of FTS complexes purified from human embryonic kidney 293T cells, we identified a new multiprotein complex, the FHF complex, containing FTS, members of the microtubule-binding Hook family of coiled-coil proteins (Hook1, Hook2, and Hook3), and a previously uncharacterized 107-kDa protein, FTS and Hook Interacting Protein (FHIP). FTS associated with a conserved C-terminal motif in Hook proteins in the yeast two-hybrid system and in tissue culture cells, and Hook proteins were found to form homo- and heterodimers. The approximately 500-kDa FHF complex contained all three Hook proteins, and small interfering RNA depletion experiments suggest that Hook proteins can interact interchangeably within this complex. Hook proteins as well as FTS interact with members of both the class B and class C components of the homotypic vesicular protein sorting (HOPS) complex. Depletion of FTS by RNA interference affects both the trafficking of epidermal growth factor from early-to-late endosome/lysosomes and the efficiency by which overexpression of the HOPS component Vps18 promotes clustering of lysosomal-associated membrane protein 1-positive endosome/lysosomes. These data suggest that the FTS/Hook/FHIP complex functions to promote vesicle trafficking and/or fusion via the HOPS complex.
-
An FTS/Hook/p107FHIP Complex Interacts with and Promotes Endosomal Clustering by the Homotypic Vacuolar Protein Sorting Complex
Molecular biology of the cell, 2008Co-Authors: Mathew E. Sowa, Jing Chen, Steven P. Gygi, J. Wade HarperAbstract:Fused Toes (FTS) is a member of a small group of inactive variant E2 ubiquitin-conjugating enzyme domain-containing proteins of unknown function. Through proteomic analysis of FTS complexes purified from human embryonic kidney 293T cells, we identified a new multiprotein complex, the FHF complex, containing FTS, members of the microtubule-binding Hook family of coiled-coil proteins (Hook1, Hook2, and Hook3), and a previously uncharacterized 107-kDa protein, FTS and Hook Interacting Protein (FHIP). FTS associated with a conserved C-terminal motif in Hook proteins in the yeast two-hybrid system and in tissue culture cells, and Hook proteins were found to form homo- and heterodimers. The approximately 500-kDa FHF complex contained all three Hook proteins, and small interfering RNA depletion experiments suggest that Hook proteins can interact interchangeably within this complex. Hook proteins as well as FTS interact with members of both the class B and class C components of the homotypic vesicular protein sorting (HOPS) complex. Depletion of FTS by RNA interference affects both the trafficking of epidermal growth factor from early-to-late endosome/lysosomes and the efficiency by which overexpression of the HOPS component Vps18 promotes clustering of lysosomal-associated membrane protein 1-positive endosome/lysosomes. These data suggest that the FTS/Hook/FHIP complex functions to promote vesicle trafficking and/or fusion via the HOPS complex.
Steven J Cooke - One of the best experts on this subject based on the ideXlab platform.
-
Influence of angler hook-set behaviour relative to hook type on capture success and incidences of deep hooking and injury in a teleost fish
Fisheries Research, 2015Co-Authors: Robert J. Lennox, Kim Whoriskey, Glenn T. Crossin, Steven J CookeAbstract:Abstract One of the primary factors associated with mortality in catch-and-release recreational fisheries is depth of hook position relative to the snout, with deeper hooking locations (i.e., gullet) increasing risk of injury to vital tissues. As a result, there have been attempts to develop angling methods and gear that are less likely to result in deep hooking. Circle hooks represent an alternative to conventional “J” style hooks (J-hooks), and in general circle hooks have been shown to reduce the tendency for deep hooking in a variety of species, which can significantly improve post-release survival. Relative to fishing with J-hooks, circle hook manufacturers typically recommend that anglers use a rod movement (i.e., hook-set) of reduced intensity and force (i.e., a light hook-set), thereby maximizing the benefit of circle hooks by reducing the tendency for deep hooking and injury. To evaluate whether hook-set technique can affect hooking and injury in fish, we tested different combinations of hooks (circle hooks and J-hooks) and hook-set techniques (e.g., light, moderate, or heavy force, or with a bobber) in an angling study for bluegill (Lepomis macrochirus) in Lake Opinicon, Ontario, Canada. Binary responses of capture success and deep hooking were analysed with logistic regression. There was no significant interaction between hook type and hook-set, but overall, J-hooks increased the odds of successfully capturing a bluegill and also the odds of deep hooking a bluegill relative to circle hooks. The bobber hook-set technique increased the odds of deep hooking a bluegill relative to the active hook-setting techniques. This study suggests both deep hooking and capture of bluegill are significantly affected by both hook types and hook-set techniques.
-
The influence of hook size, type, and location on hook retention and survival of angled bonefish (Albula vulpes)
Fisheries Research, 2012Co-Authors: Jeffrey A. Stein, Steven J Cooke, Aaron D. Shultz, Andy J. Danylchuk, Kit Hayward, Cory David SuskiAbstract:a b s t r a c t Bonefish (Albula spp.) support a circum-tropical sport fishery in which anglers predominantly release angled fish. The influence of hook location, size, and type on hook retention, post-release feeding ability and survival were evaluated. Overall, 46% of bonefish held in large holding tanks expelled hooks within a 14-day observation period. Hooks located in the lip were expelled 2.6 times more frequently than hooks located in the gut. Barbless hooks were expelled 3.9 times faster when located deep in the oral cavity compared to barbed hooks, but there was no difference in expulsion rates among barbed and barbless hooks in shallow-hooked fish. For the two hook sizes studied, hook size had no impact on hook expulsion rates or duration of hook retention regardless of hook location or type. The presence of a hook had no significant effect on weight change, indicating the presence of a hook did not impede feeding ability. No post-release mortality was observed for bonefish during the short duration of this study. Leaving a difficult to remove hook in a bonefish is recommended to increase the likelihood of post-release survival, especially in cases where the threat of bonefish predators is high.
-
Influence of Circle Hook Size on Hooking Efficiency, Injury, and Size Selectivity of Bluegill with Comments on Circle Hook Conservation Benefits in Recreational Fisheries
North American Journal of Fisheries Management, 2005Co-Authors: Steven J Cooke, Brandon L. Barthel, Michael J. Siepker, Cory David Suski, David P. PhilippAbstract:Abstract Hook size is an important consideration in the use of circle hooks as a conservation tool for minimizing the injury and mortality of marine fishes, but little is known about the role of hook size in the performance of hooks in recreational freshwater fisheries. In this study, we angled 100 bluegills Lepomis macrochirus on each of five different-sized circle hooks (1/0, 2, 6, 10, and 14). The largest hook size (1/0) had low hooking and capture efficiency but selected larger individuals. The smallest hook size also had low hooking efficiency and resulted in the selection of smaller individuals. Intermediate hook sizes captured fish of intermediate size. Jaw hooking rates generally increased with decreasing hook size, whereas roof hooking rates decreased. Gullet hooking was restricted to the three smallest hook sizes. Relative hooking depth and incidences of bleeding were uniformly low for all hook sizes. Similarly, the fish were generally easy to remove from the hook irrespective of hook size. Our ...
-
are circle hooks an effective tool for conserving marine and freshwater recreational catch and release fisheries
Aquatic Conservation-marine and Freshwater Ecosystems, 2004Co-Authors: Steven J Cooke, Cory D SuskiAbstract:Circle hooks have rapidly become popular among recreational anglers, based largely on the assumption that their use aids in the conservation of fisheries resources by reducing gut hooking, and hence mortality. In addition, circle hooks are intended to facilitate jaw hooking. Unfortunately, these assumptions have been perpetuated by anecdotal reports with very little rigorous scientific information to support these assertions. 2. A number of recently published, forthcoming, and grey literature reports provide an opportunity to review briefly and synthesize research conducted on circle hooks. We surveyed literature databases and also used questionnaires to solicit information from unpublished or in- progress circle hook research. 3. Although among studies the results have been quite disparate, overall the mortality rates were consistently lower for circle hooks than J-style hooks. In addition, circle hooks were more frequently hooked in the jaw, and less frequently hooked in the gut than conventional hook types. There is no doubt that in some marine fisheries, such as tuna, billfish, and striped bass, capture efficiency remains high and injury and mortality rates are drastically reduced. However, in other species (e.g. bluegill), injury can actually be more severe from circle hooks relative to some other hook types. In other species, such as largemouth bass, circle hooks have minimal conservation benefit, but have reduced capture efficiency relative to conventional hook designs. 4. Factors such as hook size, fishing style, fish feeding mode, and mouth morphology all appear to affect the effectiveness of circle hooks. For these reasons, it is difficult to promote the adoption of the use of circle hooks as a panacea for all fish and fisheries. Instead, we recommend that management agencies focus on recommending circle hooks only for instances for which appropriate scientific data exist. 5. The recent interest in circle hooks has been beneficial for stimulating interest and research on the role of hook designs in reducing hooking-related injury and mortality. We encourage tackle manufacturers to continue to develop new hook designs that have the potential to provide conservation benefit to caught and released fish. This paper provides direction to management
-
Injury rates, hooking efficiency and mortality potential of largemouth bass (Micropterus salmoides) captured on circle hooks and octopus hooks
Fisheries Research, 2003Co-Authors: Steven J Cooke, Michael J. Siepker, Cory David Suski, Kenneth G. OstrandAbstract:Abstract We compared the injury rates, hooking efficiency, and mortality potential of circle hooks and the more conventional octopus hooks for largemouth bass (Micropterus salmoides) captured on minnows in central Illinois. Fish captured on circle hooks (N=125) were hooked less deeply, exhibited less bleeding, and were more easily removed from the hook than were those captured on octopus hooks (N=134). The majority of fish captured using both hook types were hooked in the upper lip. Mortality rates were uniformly low for both hook types (circle, 5.1%; octopus, 6.6%). Fish that were identified as potential mortalities were typically hooked deeply in a vital organ or tissue (i.e., heart, gullet, gill arch), exhibited substantial bleeding, and were difficult to remove from the hook. No size-selective trends were noted among hook types, nor were there any differences in total length among mortalities and survivors. Capture efficiency for circle hooks was half that of octopus hooks. Our results suggest that circle hooks do provide some minimal conservation benefits relative to conventional octopus hooks despite having similar mortality rates.
J. Wade Harper - One of the best experts on this subject based on the ideXlab platform.
-
An FTS/Hook/p107FHIP Complex Interacts with and Promotes Endosomal Clustering by the Homotypic Vacuolar Protein Sorting Complex
Molecular biology of the cell, 2008Co-Authors: Mathew E. Sowa, Jing Chen, Steven P. Gygi, J. Wade HarperAbstract:Fused Toes (FTS) is a member of a small group of inactive variant E2 ubiquitin-conjugating enzyme domain-containing proteins of unknown function. Through proteomic analysis of FTS complexes purified from human embryonic kidney 293T cells, we identified a new multiprotein complex, the FHF complex, containing FTS, members of the microtubule-binding Hook family of coiled-coil proteins (Hook1, Hook2, and Hook3), and a previously uncharacterized 107-kDa protein, FTS and Hook Interacting Protein (FHIP). FTS associated with a conserved C-terminal motif in Hook proteins in the yeast two-hybrid system and in tissue culture cells, and Hook proteins were found to form homo- and heterodimers. The approximately 500-kDa FHF complex contained all three Hook proteins, and small interfering RNA depletion experiments suggest that Hook proteins can interact interchangeably within this complex. Hook proteins as well as FTS interact with members of both the class B and class C components of the homotypic vesicular protein sorting (HOPS) complex. Depletion of FTS by RNA interference affects both the trafficking of epidermal growth factor from early-to-late endosome/lysosomes and the efficiency by which overexpression of the HOPS component Vps18 promotes clustering of lysosomal-associated membrane protein 1-positive endosome/lysosomes. These data suggest that the FTS/Hook/FHIP complex functions to promote vesicle trafficking and/or fusion via the HOPS complex.
Wade J Harper - One of the best experts on this subject based on the ideXlab platform.
-
an fts hook p107fhip complex interacts with and promotes endosomal clustering by the homotypic vacuolar protein sorting complex
Molecular Biology of the Cell, 2008Co-Authors: Mathew E. Sowa, Jing Chen, Steven P. Gygi, Wade J HarperAbstract:Fused Toes (FTS) is a member of a small group of inactive variant E2 ubiquitin-conjugating enzyme domain-containing proteins of unknown function. Through proteomic analysis of FTS complexes purified from human embryonic kidney 293T cells, we identified a new multiprotein complex, the FHF complex, containing FTS, members of the microtubule-binding Hook family of coiled-coil proteins (Hook1, Hook2, and Hook3), and a previously uncharacterized 107-kDa protein, FTS and Hook Interacting Protein (FHIP). FTS associated with a conserved C-terminal motif in Hook proteins in the yeast two-hybrid system and in tissue culture cells, and Hook proteins were found to form homo- and heterodimers. The approximately 500-kDa FHF complex contained all three Hook proteins, and small interfering RNA depletion experiments suggest that Hook proteins can interact interchangeably within this complex. Hook proteins as well as FTS interact with members of both the class B and class C components of the homotypic vesicular protein sorting (HOPS) complex. Depletion of FTS by RNA interference affects both the trafficking of epidermal growth factor from early-to-late endosome/lysosomes and the efficiency by which overexpression of the HOPS component Vps18 promotes clustering of lysosomal-associated membrane protein 1-positive endosome/lysosomes. These data suggest that the FTS/Hook/FHIP complex functions to promote vesicle trafficking and/or fusion via the HOPS complex.
Steven P. Gygi - One of the best experts on this subject based on the ideXlab platform.
-
an fts hook p107fhip complex interacts with and promotes endosomal clustering by the homotypic vacuolar protein sorting complex
Molecular Biology of the Cell, 2008Co-Authors: Mathew E. Sowa, Jing Chen, Steven P. Gygi, Wade J HarperAbstract:Fused Toes (FTS) is a member of a small group of inactive variant E2 ubiquitin-conjugating enzyme domain-containing proteins of unknown function. Through proteomic analysis of FTS complexes purified from human embryonic kidney 293T cells, we identified a new multiprotein complex, the FHF complex, containing FTS, members of the microtubule-binding Hook family of coiled-coil proteins (Hook1, Hook2, and Hook3), and a previously uncharacterized 107-kDa protein, FTS and Hook Interacting Protein (FHIP). FTS associated with a conserved C-terminal motif in Hook proteins in the yeast two-hybrid system and in tissue culture cells, and Hook proteins were found to form homo- and heterodimers. The approximately 500-kDa FHF complex contained all three Hook proteins, and small interfering RNA depletion experiments suggest that Hook proteins can interact interchangeably within this complex. Hook proteins as well as FTS interact with members of both the class B and class C components of the homotypic vesicular protein sorting (HOPS) complex. Depletion of FTS by RNA interference affects both the trafficking of epidermal growth factor from early-to-late endosome/lysosomes and the efficiency by which overexpression of the HOPS component Vps18 promotes clustering of lysosomal-associated membrane protein 1-positive endosome/lysosomes. These data suggest that the FTS/Hook/FHIP complex functions to promote vesicle trafficking and/or fusion via the HOPS complex.
-
An FTS/Hook/p107FHIP Complex Interacts with and Promotes Endosomal Clustering by the Homotypic Vacuolar Protein Sorting Complex
Molecular biology of the cell, 2008Co-Authors: Mathew E. Sowa, Jing Chen, Steven P. Gygi, J. Wade HarperAbstract:Fused Toes (FTS) is a member of a small group of inactive variant E2 ubiquitin-conjugating enzyme domain-containing proteins of unknown function. Through proteomic analysis of FTS complexes purified from human embryonic kidney 293T cells, we identified a new multiprotein complex, the FHF complex, containing FTS, members of the microtubule-binding Hook family of coiled-coil proteins (Hook1, Hook2, and Hook3), and a previously uncharacterized 107-kDa protein, FTS and Hook Interacting Protein (FHIP). FTS associated with a conserved C-terminal motif in Hook proteins in the yeast two-hybrid system and in tissue culture cells, and Hook proteins were found to form homo- and heterodimers. The approximately 500-kDa FHF complex contained all three Hook proteins, and small interfering RNA depletion experiments suggest that Hook proteins can interact interchangeably within this complex. Hook proteins as well as FTS interact with members of both the class B and class C components of the homotypic vesicular protein sorting (HOPS) complex. Depletion of FTS by RNA interference affects both the trafficking of epidermal growth factor from early-to-late endosome/lysosomes and the efficiency by which overexpression of the HOPS component Vps18 promotes clustering of lysosomal-associated membrane protein 1-positive endosome/lysosomes. These data suggest that the FTS/Hook/FHIP complex functions to promote vesicle trafficking and/or fusion via the HOPS complex.
